KR20150043516A - Flagellin fusion proteins and methods of use - Google Patents

Abstract

A receptor comprising a fusion protein comprising at least one antigen that is fused to at least one domain 3 of flazelin and prazoline and wherein the isoelectric point is greater than about 7.0 activates the toll-like receptor 5. Immune Response In particular, a method of stimulating a protective immune response comprises administering a composition comprising an antigen fused to a loop of domain 3 of the flagellin.

Description

FLAGELLIN FUSION PROTEINS AND METHODS OF USE [0002]

Related application

This application is a continuation-in-part of U.S. Serial No. 13 / 931,028, filed June 28, 2013, which claims benefit of U.S. Provisional Application No. 61 / 743,165 filed on August 28, The entire teachings of this application are incorporated herein by reference.

Integration of references from ASCII text files

A sequence listing included in the following ASCII text file submitted at the same time as this application is incorporated herein by reference:

a) File name: 37101054002SEQUENCELISTING.txt; Created August 26, 2013, 1,174 KB in size.

Government support

The present invention was made with government support under HHSO1002011000011C from the Biomedical Advanced Research and Development Authority. The government has certain rights in the invention.

A composition comprising an antigen may be used to stimulate immunity against an infection caused by a disease or exposure resulting from exposure to an organism comprising an antigen. Immunity to certain diseases In particular, the antigens used in the compositions to stimulate protective immunity mimic disease-causing organisms, and the source of antigens from such organisms is the source. The composition comprising the antigen may also include an adjuvant that increases the immune response to the antigen to maximize antibody production that neutralizes the relevant antigen in the disease-causing organism. Recombinant DNA techniques have been used to generate fusion proteins including antigen and toll-like receptor agonists, particularly tosyl-like receptor 5 agonists, to increase the immune response to the antigen. However, not all antigens are suitable for fusion proteins of the present format into prazoline. Accordingly, there is a need for a novel and improved design fusion protein comprising an antigen and prazoline for use in an immune response to an antigen, in particular, a method for stimulating a protective immune response.

The present invention generally relates to compositions comprising a fusion protein that stimulates an immune response, particularly a protective immune response, in a subject, and methods of using such fusion proteins.

In an embodiment, the invention is a composition comprising a fusion protein comprising prazoline and at least one antigen having an isoelectric point of greater than about 7.0 and fused to at least one loop of domain 3 of prazoline. The fusion protein of the present invention activates toll-like receptor 5.

In another embodiment, the invention is a composition comprising a fusion protein comprising prazoline and at least one antigen having an isoelectric point of greater than about 7.5 and fused to at least one loop of domain 3 of prazoline. The fusion protein of the present invention activates toll-like receptor 5.

In another embodiment, the present invention provides a composition comprising at least three fusion proteins each activating toll-like receptor 5, wherein (a) the first fusion protein has a first prazoline and an isoelectric point greater than about 6.0 A first influenza A virus hemagglutinin antigen fused to a portion of a first flagellin; (b) the second fusion protein comprises a second plasine, and a second influenza A virus hemagglutinin having an isoelectric point of greater than about 7.0 and being fused to a portion of the second flagellin and distinguished from the first influenza A virus hemagglutinin antigen Lutinin antigens; (c) the third fusion protein comprises a first influenza B virus hemagglutinin antigen having a third prasugin and an isoelectric point greater than about 8.0 and fused to at least one loop of domain 3 of the third prasugin. .

In another further embodiment, the present invention provides a composition comprising at least four fusion proteins each activating toll-like receptor 5, wherein (a) the first fusion protein comprises a first prazoline and an isoelectric point greater than about 6.0 And a first influenza A virus hemagglutinin antigen fused to a portion of the first flazelin; (b) the second fusion protein comprises a second plasine, and a second influenza A virus hemagglutinin having an isoelectric point of greater than about 7.0 and being fused to a portion of the second flagellin and distinguished from the first influenza A virus hemagglutinin antigen Lutinin antigens; (c) the third fusion protein comprises a third plasine, and a first influenza B virus hemagglutinin antigen having an isoelectric point of greater than about 8.0 and fused to at least one loop of domain 3 of the third plasine; (d) a fourth fusion protein that activates toll-like receptor 5 has an isoelectric point of greater than about 8.0 and is fused to at least one loop of domain 3 of the fourth plasine and differentiated from the first influenza B virus hemagglutinin antigen ≪ / RTI > and a second influenza B virus hemagglutinin antigen.

In another embodiment, the invention provides a method of stimulating an immune response to an antigen in a subject, comprising administering to the subject a composition comprising a fusion protein that activates the toll-like receptor 5, Gellan, and at least one antigen having an isoelectric point of greater than about 7.0 and fused to at least one loop of domain 3 of the flagellin.

In yet another embodiment, the invention provides a method of stimulating an immune response to an antigen in a subject, comprising administering to the subject a composition comprising a fusion protein that activates the toll-like receptor 5, And at least one antigen having an isoelectric point of greater than about 7.5 and fused to at least one loop of domain 3 of the flagellin.

In yet another embodiment, the invention provides a method of stimulating an immune response in a subject, comprising administering to the subject a composition comprising at least three fusion proteins each activating the toll-like receptor 5, a) the first fusion protein comprises a first plasine, and a first influenza A virus hemagglutinin antigen having an isoelectric point of greater than about 6.0 and fused to a portion of the first prazoline; (b) the second fusion protein comprises a second plasine, and a second influenza A virus hemagglutinin having an isoelectric point of greater than about 7.0 and being fused to a portion of the second flagellin and distinguished from the first influenza A virus hemagglutinin antigen Lutinin antigens; (c) the third fusion protein comprises a first influenza B virus hemagglutinin antigen having a third prasugin and an isoelectric point greater than about 8.0 and fused to at least one loop of domain 3 of the third prasugin. Method.

In yet another embodiment, the invention provides a method of stimulating an immune response in a subject, comprising administering to the subject a composition comprising at least four fusion proteins each activating the toll-like receptor 5, a) the first fusion protein comprises a first plasine, and a first influenza A virus hemagglutinin antigen having an isoelectric point of greater than about 6.0 and fused to a portion of the first prazoline; (b) the second fusion protein comprises a second plasine, and a second influenza A virus hemagglutinin having an isoelectric point of greater than about 7.0 and being fused to a portion of the second flagellin and distinguished from the first influenza A virus hemagglutinin antigen Lutinin antigens; (c) the third fusion protein comprises a first influenza B virus hemagglutinin antigen having a third prasugin and an isoelectric point of greater than about 8.0 and fused to at least one loop of domain 3 of the third prasugin; (d) a fourth fusion protein that activates toll-like receptor 5 has an isoelectric point of greater than about 8.0 and is fused to at least one loop of domain 3 of the fourth plasine and differentiated from the first influenza B virus hemagglutinin antigen Lt; RTI ID = 0.0 > influenza B < / RTI > virus hemagglutinin antigen.

The compositions and methods of the present invention can be used to stimulate an immune response, particularly a protective immune response, in a subject. Advantages of the claimed invention include, for example, stimulating an adaptive immune response to an antigen sufficient to produce an antibody that provides a protective immunity against a disease-causing organism comprising the antigen, and an antigen having an isoelectric point greater than about 7.0 ≪ / RTI > Compositions of the present invention for use in vaccines comprising an antigen having an isoelectric point greater than about 7.0 provide an adequate balance of innate and adaptive immunostimulatory properties.

); (2) HL077의 평균 + 1 SD (

, SEQ ID NO: 146); 또는 (3) HL185의 평균 + 3 SD (

,●, SEQ ID NO: 143)를 나타낸다. 개별 마우스의 IL-6 (도 3a) 및 TNF (도 3b) 수준이 평균과 표준 오차를 나타내는 막대와 함께 도시되어 있다.
도 4a 및 4b는 생체내 TLR5 자극된 사이토킨 생성을 도시한다: B/BR (빅토리아 리니지 (Victoria lineage)) 조성물에 대한 융합 단백질 비교: R3.HA1-2 B (▼, HL169, SEQ ID NO: 147) 및 9개 아미노산 링커 B를 갖는 R3.HA1-2 B (■, HL483, SEQ ID NO: 148). R3.HA1 (●, HL185, SEQ ID NO: 143)은 양성 대조군으로서 포함되었다. 점선은 (1) 미경험 마우스의 평균 + 3 표준 편차 (SD) (

); (2) HL077의 평균 + 1 SD (

, SEQ ID NO: 146); 및 (3) HL185의 평균 + 3 SD (

, ●, SEQ ID NO: 143)을 나타낸다. 개별 마우스의 IL-6 (도 4a) 및 TNF (도 4b) 수준이 평균과 표준 오차를 나타내는 막대와 함께 도시된다.
도 5a 및 5b는 생체내 TLR5 자극된 사이토킨 생성을 보여준다: 추가적인 음전하를 갖는 융합 단백질 조성물의 비교. 점선은 면역원성과 상관관계에 있는 사이토킨 수준의 역치를 나타낸다. 개별 마우스의 IL-6 (도 5a) 및 TNF (도 5b) 수준이 평균과 표준 오차를 나타내는 막대와 함께 도시된다. B/FL (야마가타 리니지)에 대한 포맷을 비교하였다: 9aa (아미노산) 링커 (SEQ ID NO: 123) B를 갖는 R3.HA1-2 B (■, HL352, SEQ ID NO: 125) 및 링커내에 추가적인 음전하가 유입된 동일한 포맷 (●, HL610, SEQ ID NO: 149). B/BR (야마가타 리니지)에 대한 포맷을 비교하였다: 9aa (아미노산) 링커 (SEQ ID NO: 123) B를 갖는 R3.HA1-2 B (▲, HL169, SEQ ID NO: 147) 및 링커내에 추가적인 음전하가 유입된 동일한 포맷 (◆, HL611, SEQ ID NO: 150). R3.HA1 (●, HL185, SEQ ID NO: 143)를 양성 대조군으로서 미경험물 (■)을 음성 대조군으로서 포함시켰다.
도 6은 링커에 음으로 하전된 아미노산을 함유하는 2개의 B/FL 조성물의 유사한 NIA 활성을 도시한다: B/Florida/4/06 R3 융합 단백질 조성물 HL352 (○, SEQ ID NO: 125) 및 HL610 (□, SEQ ID NO: 149).
도 7은 HA의 구상 헤드의 일부를 포함하는 HA의 일부에서 추가적인 음으로 하전된 아미노산 잔기 (SEQ ID NO: 153)를 사용하거나 사용하지 않는 B/BR 조성물의 NIA 활성 비교를 도시한다: B/Brisbane/60/08 R3 융합 단백질 조성물 HL169 (○, SEQ ID NO: 147), HL483 (SEQ ID NO: 148) (□, SEQ ID NO: 123의 9개 아미노산 링커를 가짐), 및 HL611 (SEQ ID NO: 150) (Δ, SEQ ID NO: 153의 9개 아미노산 연장되고 기타 음으로 하전된 아미노산을 가짐).
도 8a 및 8b는 생체내 TLR5 자극된 사이토킨 생성을 보여준다: 융합 단백질 조성물의 비교: B/FL (야마가타 리니지) R3.HA B (■, HL352, SEQ ID NO: 125) 및 D3Ins.HA B (▲, HL656, SEQ ID NO: 151) 및 B/BR (빅토리아 리니지) R3.HA B (▲, HL169, SEQ ID NO: 147) 및 D3Ins.HA B (▼, HL657, SEQ ID NO: 128). R3.HA1 (●, HL185, SEQ ID NO: 143)은 양성 대조군으로서 포함되었다. 점선은 면역원성과 상관관계에 있는 사이토킨의 역치를 나타낸다. 개별 마우스의 IL-6 (A) 및 TNF (B) 수준이 평균과 표준 오차를 나타내는 막대와 함께 도시된다.
도 9a 내지 9c는 B/Florida/4/06 (○, HL352, SEQ ID NO: 125 및 □, HL656, SEQ ID NO: 151) (A), B/Brisbane/60/08 (□, HL611, SEQ ID NO: 150 및 ○, HL657, SEQ ID NO: 128) (B), 또는 B/Wisconsin/1/10 (▲, HL724, SEQ ID NO: 152 및 ○, HL772, SEQ ID NO: 126) (C)의 융합 단백질 조성물의 NIA 활성 비교를 보여준다.
도 10은 D3Ins B/Fl 조성물이 프라젤린의 R3 포맷에 융합된 HA를 포함하는 융합 단백질보다 우수한 MN 역가를 유도함을 보여준다: HL352 (SEQ ID NO: 125) (●, SEQ ID NO: 123의 9 연장부를 갖는 R3), HL610 (SEQ ID NO: 149) (○, SEQ ID NO: 153의 9개 아미노산 링커 및 추가로 음으로 하전된 아미노산을 갖는 R3), 또는 HL656 (SEQ ID NO: 151) (○, SEQ ID NO: 123의 9개 아미노산 링커를 갖는 D3Ins). 데이타는 상기 각 군을 혈청전환 비율 (약 80 또는 그 초과의 NM 역가를 갖는 마우스의 퍼센트 (%)) 및 GMT에 대한 개별 마우스의 역가로서 도시된다.
도 11은 B/Wisconsin/1/2010 포맷의 상대적 면역원성을 보여준다: R3 B/WI (●, HL719, SEQ ID NO: 154, 음의 링커를 갖는 R3), R3 B/WI (■, HL724, SEQ ID NO: 152, 아미노산 연장부에 추가의 음전하를 갖는 R3 작제물 포맷), D3Ins B WI (▲, HL772, SEQ ID NO: 126 또는 F147 완충제 (●). 데이타는 GMT를 이용한 개별 마우스의 역가로서 도시된다. 통계적 차이를 1-웨이 ANOVA/Tukey 검사로 측정하였다. *, p < 0.05, ***, p < 0.001.
도 12는 일가 flu B (인플루엔자 B) 조성물의 HAI 역가를 도시한다: B/Brisbane/60/08-유사 바이러스 (B/Brisbane/60/08 또는 B/BR, HL657, SEQ ID NO: 128; B/Hong Hong/259/10 또는 B/HK, HL774, SEQ ID NO: 157; 및 B/Bangladesh/5945/09 또는 B/BD, HL787, SEQ ID NO: 158)의 R3 포맷 (HL611, SEQ ID NO: 150; HL753, SEQ ID NO: 155; HL742, SEQ ID NO: 156) 또는 D3Ins 포맷 조성물. 대조군은 FLUVIRIN® 또는 F147 완충제를 포함하였다. 데이타는 GMT를 이용한 개별 마우스의 역가로서 도시된다. 통계적 차이는 2-웨이 ANOVA/Tukey 검사로 측정하였으며, *, p < 0.05, **, p < 0.01이다.
도 13a 및 13b는 생체내 TLR5 자극된 사이토킨 생성을 도시한다: D3Ins 포맷 융합 단백질의 변이 비교: B Wisconsin (야마가타 리니지) D3I-o1 (HL772, SEQ ID NO: 126), D3I-s1 (HL848, SEQ ID NO: 160), 및 D3I-i1 (HL849, SEQ ID NO: 159). R3.HA1 (HL185, SEQ ID NO: 143)은 양성 대조군으로서 포함되었다.
도 14는 항원을 포함하는 융합 단백질의 생성을 위한 프라젤린의 구조 즉, 프라젤린 (SEQ ID NO: 2)에서 도메인 0, 1, 2, 및 3 및 삽입 부위를 묘사한다. 아미노산 번호에 대한 참조는 SEQ ID NO: 2에 대해 이루어진다.
도 15a 및 15b는 생체내 TLR5 자극된 사이토킨 생성을 도시한다: D3I 및 D2I 융합 단백질 작제물의 변이의 비교: B Wisconsin (야마가타 리니지) D3I-o1 (HL772, SEQ ID NO: 126), D2I-o1 (HL825, SEQ ID NO: 161), D2I-o2 (HL826, SEQ ID NO: 162), D2I-o3 (HL827, SEQ ID NO: 163), D1I-o1 (HL828, SEQ ID NO: 164) 및 D2I-i1 (HL850, SEQ ID NO: 165) 및 B Brisbane (빅토리아 리니지) D3I-o1 (HL657, SEQ ID NO: 128), D2I-o1 (HL733, SEQ ID NO: 166), D2I-o1 (HL856, SEQ ID NO: 167) 및 D2I-o2 (HL857, SEQ ID NO: 168). R3.HA1 (HL185, SEQ ID NO: 143)는 양성 대조군으로서 포함되었다. 개별 마우스의 IL-6 (도 15a) 및 TNF-알파 (도 15b) 수준이 평균과 표준 오차를 나타내는 막대와 함께 도시된다.
도 16a 및 16b는 생체내 TLR5 자극된 사이토킨 생성을 보여준다: D3I 및 D2I 융합 단백질 작제물의 변이 비교: B Wisconsin (야마가타 리니지)가 도 16a에서 비교되었으며: D3I-o1 (HL772, SEQ ID NO: 126), D3I-o2 (HL888, SEQ ID NO: 169), D2I-c1 (HL890, SEQ ID NO: 170), D2I-i2 (HL892, SEQ ID NO: 171); B Brisbane (빅토리아 리니지)는 도 16b에서 비교되었다: D3I-o1 (HL657, SEQ ID NO: 128), D2I-o3 (HL858, SEQ ID NO: 172), D3I-s1 (HL860, SEQ ID NO: 173), D3I-o2 (HL889, SEQ ID NO: 174), D2I-c1 (HL891, SEQ ID NO: 175) 및 D2I-i2 (HL893, SEQ ID NO: 176). R3.HA1 (HL185, SEQ ID NO: 143)을 양성 대조군으로서 포함시켰다. 개별 마우스로부터의 IL6 농도가 평균과 표준 오차를 나타내는 막대와 함께 도시된다.
도 17은 삽입 변이체 (B/Wisconsin/1/2010)에 대한 NIA 검정을 보여준다: R3 포맷 (▲, HL724, SEQ ID NO: 152)과 비교하여 D3Ins (○, HL772, D3I-o1, SEQ ID NO: 126), 다양한 D2Ins (Δ, HL825, D2I-o1, SEQ ID NO: 161; ◇, HL826, D2I-o2, SEQ ID NO: 162; ●, HL827, D2I-o3, SEQ ID NO: 163), 및 D1Ins (■, HL828, D1I-o1, SEQ ID NO: 164).
도 18a 및 18b는 D3I 포맷과 비교한 B/Wisconsin/1/2010 D2I 변이체에 대한 NIA 검정을 보여준다. A) B/Wisconsin/1/2010 D3I 삽입 융합 단백질: D2I-i1 (●, HL850, SEQ ID NO: 165)와 D2I (■, HL854, SEQ ID NO: 179) 융합 단백질과 비교한 D3I-o1 (○, HL772, SEQ ID NO: 126), D3I-s1 (Δ, HL848, SEQ ID NO: 160), D3I-i1 (◇, HL849, SEQ ID NO: 159), 및 D3I (▲, HL864, SEQ ID NO: 177). B) B/Wisconsin/1/2010 D3I 삽입 융합 단백질: D2I-i2 (◇ HL892, SEQ ID NO: 171)와 비교한 D3I-o1 (○, HL772, SEQ ID NO: 126), D3I-o2 (□, HL888, SEQ ID NO: 169), 및 D3I-c1 (Δ, HL890, SEQ ID NO: 170).
도 19a는 (B/Brisbane/60/2008) D3I 융합 단백질에 대한 NIA 검정 데이타를 보여준다: R3 (□, HL611, SEQ ID NO: 150) 융합 단백질과 비교한 D3I-o1 (○, HL657, SEQ ID NO: 128) 및 D3I-i1 (■, HL861, SEQ ID NO: 180).
도 19b는 융합 단백질 삽입 변이체와 비교한 B/Brisbane/60/2008 R3 (□, HL611, SEQ ID NO: 150) 융합 단백질에 대한 NIA 검정을 보여준다: D3I-o1 (○, HL657, SEQ ID NO: 128), D2I-o1 (Δ, HL733, SEQ ID NO: 166), D2I-o1 (■, HL856, SEQ ID NO: 167), D2I-o2 (▲, HL857, SEQ ID NO: 168), 및 D2I-i1 (◆, HL862, SEQ ID NO: 181).
도 20은 B/Brisbane/60/2008 D3I 융합 단백질에 대한 NIA 검정을 보여준다: D2I 융합 단백질과 비교한 D3I-o1 (○, HL657, SEQ ID NO: 128) 및 D2I-o3 (□, HL858, SEQ ID NO: 172): D3I-s1 (Δ, HL860, SEQ ID NO: 173), D3I-o2 (HL889, SEQ ID NO: 174), D2I-c1 (HL891, SEQ ID NO: 175), D2I-i2 (HL893, SEQ ID NO: 176), 및 D2I-i1 (HL862, SEQ ID NO: 181).
도 21a 및 21b는 A) D3I-o1, HL772, SEQ ID NO: 126; D3I-i1, HL849, SEQ ID NO: 159 및 D2I-i1, HL850, SEQ ID NO: 165을 포함하는 B/Wisconsin/1/2010 (B/WI) 융합 단백질 조성물 또는 B) B/Sichuan/379/1999 D3I-o1 (HL863, SEQ ID NO: 182) 또는 D3I-i1(HL903, SEQ ID NO: 183)로의 처리에 대한 마우스에서 GMT로서 표현된 HAI 연구가 도시된다. 양성 (HA HU 및 HA0 WI) 및 음성 F147 (완충제) 대조군이 또한 포함되었다. 혈청전환 비율 (약 40 또는 그 초과의 HAI를 나타내는 마우스의 퍼센트)이 또한 제공되었다. ***, ANOVA 검사에서 p < 0.001 대 F147 군.
도 22는 B/Wisconsin/1/2010 (D3Ins B/WI, HL772, SEQ ID NO: 126); B/Hubei-Wujiagang/158/2009 (D3Ins B/HU HL869, SEQ ID NO: 184) 및 B/Texas/6/2011 (D3Ins B/TX HL871, SEQ ID NO: 185)로의 처리 후 마우스 혈청의 HAI 역가를 보여준다. 가로선은 GMT (상기 수)를 나타낸다. 혈청전환율이 도시된다.
도 23은 토끼에서 B Brisbane 또는 Bangladesh의 D3Ins 융합 단백질 조성물에 의해 유도된 HAI 역가를 보여준다. FLUVIRIN®는 양성 대조군으로서 포함되며, F147 완충제는 음성 대조군이다. 데이타는 개별 토끼의 역가로서 막대로 도시된다. 가로선은 GMT (상기 수)를 나타낸다. 혈청전환 백분율이 도시된다.
도 24는 융합 단백질 조성물 STF2D3InsB/SI (HL863, SEQ ID NO: 182) 또는 포뮬레이션 완충제 (F147)로의 처리 후 마우스 혈청의 HAI 역가를 도시한다. 데이타는 상기 나타낸 혈청전환 및 GMT로 개별적으로 플롯팅하였다.
도 25a 및 25b는 B/Sichuan/379/99 바이러스로 감작한 마우스에서 융합 단백질 D3Ins B/SI 99 (HL863, SEQ ID NO: 182) 조성물의 처리 효율을 보여준다. 생존율 (도 25a) 및 중량 (초기 중량의 평균 백분율) (도 25b)이 도시된다.
도 26은 융합 단백질 R3 B Wisconsin (HL724, SEQ ID NO: 152) 및 D3Ins B Wisconsin (HL772, SEQ ID NO: 126)에 의해 유도된 HAI 역가를 보여준다. CBER HA는 양성 대조군으로서 포함되며, F147 완충제는 음성 대조군으로서 포함된다. 데이타는 기하 평균 및 혈청전환 백분율을 나타내는 수 및 막대를 이용하여 개별 토끼의 역가로서 도시된다.
도 27은 융합 단백질 STF2D3Ins B/WI (HL772, SEQ ID NO: 126), 양성 대조군 휴베이 (Hubei) 바이러스, 또는 포뮬레이션 완충제 (F147)로의 처리 후 토끼 혈청의 HAI 역가를 보여준다. 값은 GMT 및 혈청전환으로 개별적으로 플롯팅된다.
도 28a-28c는 토끼에서 HL772 융합 단백질 (SEQ ID NO: 126) 또는 완충제 대조군 (F147)의 반응원성 (reactogenicity)을 보여준다. 10마리 토끼 군을 x-축에 지시된 용량으로 1회 면역화시켰다. 도 28a는 면역화 후 약 24 시간째에 측정된 식품 소비를 묘사한다. 도 28b는 면역화후 약 6 시간째에 직장으로 측정된 온도를 묘사한다. 도 28c는 초기 면역화 후 (또한, "프라임"으로서 불림), 프라임 후 약 24시간째에 취해진 혈청으로부터 측정된 CRP를 묘사한다. 모든 측정 데이타는 평균 및 평균의 표준 오차를 나타내는 선으로 개별 토끼의 결과로서 도시된다. 점선은 포뮬라 대조군 토끼로부터의 데이타를 사용하여 계산된 안전성 역치를 나타낸다.
도 29는 공지된 결정 구조를 기반으로 하는 S. 타이피무리움 FljC (S. typhimurium FljC) (SEQ ID NO: 1)에 대한 도메인 3의 루프 및 S. 타이파무리움 FljB (SEQ ID NO: 2)의 예측된 루프를 묘사한다.
도 30은 도메인 3의 루프에서 삽입 부위를 포함하는, 항원과의 융합을 위한 S. 타이피무리움 FljB (SEQ ID NO: 2)의 도메인 0, 1, 2 및 3에서 예측된 삽입 부위를 묘사한다. 도메인 0은 아미노산 잔기 1-46 및 아미노산 잔기 465-506으로 예측되고; 도메인 1은 아미노산 잔기 47-176 및 아미노산 잔기 415-464로 예측되고; 도메인 2는 아미노산 잔기 177-190 및 아미노산 잔기 292-414로 예측되고; 도메인 3은 아미노산 잔기 191-291로 예측된다. 도메인 0, 1, 2 및 3 및 삽입 부위 간의 경계부의 아미노산 수를 또한 나타낸다.
도 31은 프라젤린의 아미노-도메인 0, 아미노-도메인 1, 아미노-도메인 2, 카르복시-도메인 2, 카르복시-도메인 1 및 카르복시-도메인 0을 차례로 포함하는 융합 단백질 및 프라젤린 작제물 (SEQ ID NO: 283)의 도메인 (D0, D1, D2, D3)을 묘사한다. 항원 (Ag)은 프라젤린 작제물의 도메인 2의 아미노-말단과 카르복시-말단 사이에 삽입된다. 프라젤린 작제물은 "R3 작제물" (SEQ ID NO: 283)로서 본원에서 불리며, 자연 발생 프라젤린 (SEQ ID NO: 2)에는 존재하는 도메인 3이 결여되어 있다.
도 32는 프라젤린의 아미노-도메인 0, 아미노-도메인 1, 아미노-도메인 2, 카르복시-도메인 2, 카르복시-도메인 1 및 카르복시-도메인 0을 차례로 포함하는 융합 단백질 및 프라젤린 작제물 (SEQ ID NO: 284)의 도메인 (D0, D1, D2, D3)을 묘사한다. 두 항원 (Ag)이 융합 단백질에 존재한다. 한 항원은 프라젤린 작제물의 아미노-도메인 2와 카르복시-도메인 2 사이에 융합된다. 또 다른 항원은 프라젤린 작제물의 도메인 0의 카르복시-말단 아미노산에 융합된다. 프라젤린 작제물은 "R3-2xAg" 작제물로서 본원에서 불리며, 자연 발생 프라젤린 (SEQ ID NO: 2)의 도메인 3가 결여되어 있다.Figure 1 depicts a hemagglutinin (HA) trimer, a full-length HA1 subunit having HA1 globular head subunit (distal membrane), and an HA2 subunit (proximal subunit). Some of the HA1 subunits referred to as "HA1-1" and "HA1-2" are depicted. A portion of the HA referred to as "HA 1-3" was used as a negative control and lacked sufficient secondary structure to maintain essentially the tertiary structure of the spherical head of the HA portion.
2A shows a fusion protein comprising a fragment of the R3 format and a portion of the HA (SEQ ID NO: 45) and lacking a negatively charged linker (SEQ ID NO: 123) between HA antigen and Praseline NO: 122) do not induce an immunogenic response to the HA component of the fusion protein. Serum HAI antibody titers were determined by HAI assay for B / Florida / 4/06 and were calculated as HL199 (SEQ ID NO: 45) or 10 μg (▲) or 3 μg (GMT, horizontal line) for HL098 (SEQ ID NO: 122) of the wild-type (▼). The F147 formulation buffer was used as a negative control (◆). BV (baculovirus) expressing HAO (O, full length HA) was used as a positive control.
Figure 2b shows that the inclusion of an amino acid linker (SEQ ID NO: 123) with a net negative charge in the fusion protein (SEQ ID NO: 122) depicted in Figure 2A increased the immunogenicity of the fusion protein to the HA element. Serum antibody titer was measured by MN assay for B / Florida / 4/06 virus and using GMT (horizontal line) for HL199 (●, SEQ ID NO: 145) or HL352 (▼, SEQ ID NO: 125) And plotted separately. Controls included BV (baculovirus) expressing formulation buffer (+, F147, negative) and HAO (*, full length HA, positive).
Figures 3a and 3b show TLR5 stimulated cytokine production in vivo: B / FL (Fusion protein comparison for Yamagata lineage composition: R3.HA1-2B (I, HL098, SEQ ID NO: 122) and HL185, SEQ ID NO: 143) with 9 amino acid linkers B was included as a positive control group, and the dotted line indicates (1, ) Mean + 3 standard deviations (SD) of inexperienced mice

); (2) Average of HL077 + 1 SD (

, SEQ ID NO: 146); Or (3) an average of HL185 + 3 SD (

, ●, SEQ ID NO: 143). IL-6 (FIG. 3a) and TNF (FIG. 3b) levels of individual mice are shown with bars indicating mean and standard error.
Figures 4a and 4b illustrate TLR5 stimulated cytokine production in vivo: Fusion protein comparison for B / BR (Victoria lineage) composition: R3.HA1-2B (?, HL169, SEQ ID NO: 147 ) And R3.HA1-2B (9, HL483, SEQ ID NO: 148) with 9 amino acid linkers B. R3.HA1 (•, HL185, SEQ ID NO: 143) was included as a positive control. The dotted line indicates (1) mean + 3 standard deviation (SD) of inexperienced mice

); (2) Average of HL077 + 1 SD (

, SEQ ID NO: 146); And (3) an average of HL185 + 3 SD (

, ●, SEQ ID NO: 143). IL-6 (Figure 4a) and TNF (Figure 4b) levels of individual mice are shown with bars showing mean and standard error.
Figures 5a and 5b show in vivo TLR5 stimulated cytokine production: comparison of fusion protein compositions with additional negative charge. The dotted line represents the threshold of cytokine levels correlated with immunogenicity. IL-6 (Figure 5a) and TNF (Figure 5b) levels of individual mice are shown with bars showing mean and standard error. (HL352, SEQ ID NO: 125) with 9aa (amino acid) linker (SEQ ID NO: 123) B and an additional The same format in which the negative charge is introduced (●, HL610, SEQ ID NO: 149). (HL169, SEQ ID NO: 147) with 9aa (amino acid) linker (SEQ ID NO: 123) B and additional (◆, HL611, SEQ ID NO: 150) in which a negative charge is introduced. R3. HA1 (占, HL185, SEQ ID NO: 143) was included as a negative control as a negative control (?) As a negative control.
Figure 6 shows a similar NIA activity of two B / FL compositions containing negatively charged amino acids in the linker: B / Florida / 4/06 R3 fusion protein composition HL352 (O, SEQ ID NO: 125) and HL610 (?, SEQ ID NO: 149).
Figure 7 shows NIA activity comparisons of B / BR compositions with or without additional negatively charged amino acid residues (SEQ ID NO: 153) in a portion of the HA containing part of the spherical head of HA: B / (SEQ ID NO: 148) (having the 9 amino acid linker of SEQ ID NO: 123), and HL611 (SEQ ID NO: 147), the Brisbane / 60/08 R3 fusion protein composition HL169 NO: 150) (delta, 9 amino acids of SEQ ID NO: 153, with other negatively charged amino acids).
Figures 8A and 8B show in vivo TLR5 stimulated cytokine production: comparison of fusion protein compositions: B / FL (Yamagata Lineage) R3.HA B (HL352, SEQ ID NO: 125) and D3Ins.HA B HL656, SEQ ID NO: 151) and B / BR (Victoria Lineage) R3.HA B (▲, HL169, SEQ ID NO: 147) and D3Ins.HA B (▼, HL657, SEQ ID NO: 128). R3.HA1 (•, HL185, SEQ ID NO: 143) was included as a positive control. The dotted line represents the threshold of cytokines correlated with immunogenicity. IL-6 (A) and TNF (B) levels in individual mice are shown with bars indicating mean and standard error.
Figures 9a to 9c illustrate B / Florida / 4/06 (O, HL352, SEQ ID NO: 125 and □, HL656, SEQ ID NO: 151) (A), B / Brisbane / 60/08 HL724, SEQ ID NO: 152 and?, HL772, SEQ ID NO: 126) (B), or B / Wisconsin / ) &Lt; / RTI &gt; of the fusion protein composition.
Figure 10 shows that the D3Ins B / Fl composition induces an MN titer that is superior to the fusion protein comprising HA fused to the R3 format of prazoline: HL352 (SEQ ID NO: 125) (•, 9 of SEQ ID NO: 123 (SEQ ID NO: 149) (O, a nine amino acid linker of SEQ ID NO: 153 and R3 with an additional negatively charged amino acid), or HL656 (SEQ ID NO: 151) O, D3Ins with 9 amino acid linkers of SEQ ID NO: 123). Data are shown for each of the above groups as the serum conversion ratios (percent (%) of mice with NM titer of about 80 or greater) and titer of individual mice for GMT.
Figure 11 shows the relative immunogenicity of the B / Wisconsin / 1/2010 format: R3 B / WI (3, HL719, SEQ ID NO: 154, R3 with negative linker) D3Ins B WI (▲, HL772, SEQ ID NO: 126 or F147 buffer (.)). Data were obtained from the individual mouse titer using GMT Statistical differences were determined by the 1-way ANOVA / Tukey test. *, P <0.05, ***, p <0.001.
B / Brisbane / 60/08-like virus (B / Brisbane / 60/08 or B / BR, HL657, SEQ ID NO: 128; B (HL611, SEQ ID NO: 157) of the amino acid sequence of SEQ ID NO: / Hong Hong / 259/10 or B / HK, HL774, SEQ ID NO: 157 and B / Bangladesh / 5945/09 or B / BD, HL787, SEQ ID NO: : 150; HL753, SEQ ID NO: 155; HL742, SEQ ID NO: 156) or D3Ins format composition. Controls included FLUVIRIN® or F147 buffer. Data are shown as the titer of individual mice using GMT. Statistical differences were measured by 2-way ANOVA / Tukey test, *, p <0.05, **, p <0.01.
Figures 13a and 13b illustrate TLR5 stimulated cytokine production in vivo: Comparison of mutations in D3Ins format fusion proteins: B Wisconsin (Yamagata Lineage) D3I-o1 (HL772, SEQ ID NO: 126), D3I-s1 (HL848, SEQ ID NO: 160), and D3I-i1 (HL849, SEQ ID NO: 159). R3.HA1 (HL185, SEQ ID NO: 143) was included as a positive control.
14 depicts domains 0, 1, 2, and 3 and insertion sites in the structure of praxelin, i.e., praxelin (SEQ ID NO: 2), for the production of a fusion protein comprising an antigen. A reference to the amino acid number is made for SEQ ID NO: 2.
15A and 15B illustrate TLR5 stimulated cytokine production in vivo: comparison of mutations of D3I and D2I fusion protein constructs: B Wisconsin (Yamagata Lineage) D3I-o1 (HL772, SEQ ID NO: 126), D2I-o1 (HL825, SEQ ID NO: 161), D2I-o2 (HL826, SEQ ID NO: 162), D2I-o3 (HL827, SEQ ID NO: (HL850, SEQ ID NO: 165) and B Brisbane (Victoria Lineage) D3I-o1 (HL657, SEQ ID NO: 128), D2I-o1 (HL733, SEQ ID NO: 166), D2I- SEQ ID NO: 167) and D2I-o2 (HL857, SEQ ID NO: 168). R3.HA1 (HL185, SEQ ID NO: 143) was included as a positive control. IL-6 (Figure 15a) and TNF-alpha (Figure 15b) levels of individual mice are shown with bars showing mean and standard error.
Figures 16a and 16b show in vivo TLR5 stimulated cytokine production: Comparison of mutations in D3I and D2I fusion protein constructs: B Wisconsin (Yamagata Lineage) was compared in Figure 16a: D3I-o1 (HL772, SEQ ID NO: 126 ), D3I-o2 (HL888, SEQ ID NO: 169), D2I-cl (HL890, SEQ ID NO: 170), D2I-i2 (HL892, SEQ ID NO: 171); B Brisbane (Victoria Lineage) was compared in Figure 16b: D3I-o1 (HL657, SEQ ID NO: 128), D2I-o3 (HL858, SEQ ID NO: 172), D3I-s1 ), D3I-o2 (HL889, SEQ ID NO: 174), D2I-cl (HL891, SEQ ID NO: 175) and D2I-i2 (HL893, SEQ ID NO: 176). R3.HA1 (HL185, SEQ ID NO: 143) was included as a positive control. The IL6 concentration from individual mice is shown with bars indicating mean and standard error.
Figure 17 shows the NIA assay for insertions (B / Wisconsin / 1/2010): D3Ins (O, HL772, D3I-o1, SEQ ID NO: 152) (SEQ ID NO: 163), various D2Ins (?, HL825, D2I-o1, SEQ ID NO: 161; And D1Ins (1, HL828, D1I-o1, SEQ ID NO: 164).
Figures 18a and 18b show NIA assays for B / Wisconsin / 1/2010 D2I variants compared to the D3I format. (D3I-o1 (SEQ ID NO: 165) and D2I (HL854, SEQ ID NO: 179) fusion proteins compared to the D3I fusion protein: D2I- Hl864, SEQ ID NO: 126), D3I-s1 (?, HL848, SEQ ID NO: 160), D3I-i1 (?, HL849, SEQ ID NO: NO: 177). B1) D3I-o1 (O, HL772, SEQ ID NO: 126), D3I-o2 (□) compared with B / Wisconsin / 1/2010 D3I insertion fusion protein: D2I-i2 (◇ HL892, SEQ ID NO: , HL888, SEQ ID NO: 169), and D3I-cl (Δ, HL890, SEQ ID NO: 170).
Figure 19a shows the NIA assay data for the D3I fusion protein (B / Brisbane / 60/2008): D3I-o1 (O, HL657, SEQ ID NO: 128) and D3I-i1 (I, HL861, SEQ ID NO: 180).
19B shows NIA assays for the fusion proteins B / Brisbane / 60/2008 R3 (□, HL611, SEQ ID NO: 150) compared to fusion protein insertion variants: D3I-o1 (○, HL657, SEQ ID NO: Hl857, SEQ ID NO: 168), and D2I (SEQ ID NO: 166), D2I-o1 (?, HL853, SEQ ID NO: -i1 (◆, HL862, SEQ ID NO: 181).
Figure 20 shows NIA assays for B / Brisbane / 60/2008 D3I fusion proteins: D3I-o1 (O, HL657, SEQ ID NO: 128) and D2I-o3 (□, HL858, SEQ (HL891, SEQ ID NO: 175), D2I-i2 (SEQ ID NO: 173), D3I- (HL893, SEQ ID NO: 176), and D2I-i1 (HL862, SEQ ID NO: 181).
Figures 21A and 21B show A) D3I-o1, HL772, SEQ ID NO: 126; B / Wisconsin / 1/2010 (B / WI) fusion protein composition comprising D3I-i1, HL849, SEQ ID NO: 159 and D2I-i1, HL850, SEQ ID NO: 165 or B) B / Sichuan / 379 / The HAI study is shown as GMT in mice for treatment with 1999 D3I-o1 (HL863, SEQ ID NO: 182) or D3I-i1 (HL903, SEQ ID NO: 183). Positive (HA HU and HA0 WI) and negative F147 (buffer) controls were also included. Serum conversion ratios (percent of mice representing about 40 or more HAIs) were also provided. ***, p <0.001 vs F147 in ANOVA test.
22 shows B / Wisconsin / 1/2010 (D3Ins B / WI, HL772, SEQ ID NO: 126); HAI (SEQ ID NO: 184) of mouse serum after treatment with B / Hubei-Wujiagang / 158/2009 (D3Ins B / HU HL869, SEQ ID NO: 184) and B / Texas / 6 / It shows the activity. The horizontal line indicates GMT (the above number). Serum conversion is shown.
Figure 23 shows the HAI titers induced by the D3Ins fusion protein composition of B Brisbane or Bangladesh in rabbits. FLUVIRIN® is included as a positive control and F147 buffer is a negative control. Data are shown as bars as potencies for individual rabbits. The horizontal line indicates GMT (the above number). Serum conversion percentages are shown.
Figure 24 shows the HAI titer of mouse serum after treatment with the fusion protein composition STF2D3InsB / SI (HL863, SEQ ID NO: 182) or formulation buffer (F147). Data were plotted separately with the indicated serum conversion and GMT.
25a and 25b show the treatment efficiency of the fusion protein D3Ins B / SI 99 (HL863, SEQ ID NO: 182) composition in mice sensitized with B / Sichuan / 379/99 virus. Survival (FIG. 25A) and weight (average percentage of initial weight) (FIG. 25B) are shown.
Figure 26 shows the HAI titers induced by the fusion proteins R3B Wisconsin (HL724, SEQ ID NO: 152) and D3Ins B Wisconsin (HL772, SEQ ID NO: 126). CBER HA is included as a positive control and F147 buffer is included as a negative control. Data are shown as titers of individual rabbits using numbers and bars representing the geometric mean and serum conversion percentages.
Figure 27 shows the HAI titers of rabbit sera after treatment with the fusion protein STF2D3InsB / WI (HL772, SEQ ID NO: 126), positive control Hubei virus, or formulation buffer (F147). Values are plotted individually with GMT and serum conversion.
Figures 28a-28c show the reactogenicity of the HL772 fusion protein (SEQ ID NO: 126) or the buffer control (F147) in rabbits. Groups of 10 rabbits were immunized once with the indicated doses on the x-axis. Figure 28a depicts food consumption measured approximately 24 hours after immunization. Figure 28b depicts the temperature measured at the rectum about 6 hours after immunization. Figure 28c depicts the CRP measured from serum taken after approximately 24 hours post prime (also referred to as "prime") after initial immunization. All measurement data are shown as a result of individual rabbits as a line representing the mean and standard error of the mean. The dotted line represents the safety threshold calculated using data from the formula control rabbit.
Figure 29 shows a loop of domain 3 for a S. typhimurium FljC (SEQ ID NO: 1) based on a known crystal structure and a loop of S. typhimurium FljB (SEQ ID NO: 2). &Lt; / RTI &gt;
Figure 30 depicts the predicted insertion sites in domains 0, 1, 2 and 3 of S. typhimurium FljB (SEQ ID NO: 2) for fusion with an antigen, including the insertion site in the loop of domain 3 do. Domain 0 is predicted as amino acid residue 1-46 and amino acid residue 465-506; Domain 1 is predicted as amino acid residue 47-176 and amino acid residue 415-464; Domain 2 is predicted as amino acid residues 177-190 and amino acid residues 292-414; Domain 3 is predicted as amino acid residue 191-291. It also shows the number of amino acids at the border between domains 0, 1, 2 and 3 and the insertion site.
31 shows a fusion protein and a fragment construct (SEQ ID NO &lt; RTI ID = 0.0 &gt; NO) &lt; / RTI &gt; comprising a fusion protein comprising in turn the amino-domain 0, amino-domain 1, amino- domain 2, carboxy- domain 1, carboxy- : 283) of domains D0, D1, D2, D3. The antigen (Ag) is inserted between the amino-terminal and carboxy-terminal of domain 2 of the prazoline construct. The prazoline construct is referred to herein as the &quot; R3 construct "(SEQ ID NO: 283) and lacks domain 3 present in naturally occurring prazylene (SEQ ID NO: 2).
Figure 32 shows a fusion protein and a fragment construct (SEQ ID NO &lt; RTI ID = 0.0 &gt; NO: &lt; / RTI & : D0, D2, D3) of the cells D0, D2, D4, and D4. Two antigens (Ag) are present in the fusion protein. One antigen is fused between amino-domain 2 and carboxy-domain 2 of the prazoline construct. Another antigen is fused to the carboxy-terminal amino acid of domain 0 of the prazoline construct. The prazoline construct is referred to herein as the "R3-2xAg" construct and lacks domain 3 of naturally occurring prazoline (SEQ ID NO: 2).

DETAILED DESCRIPTION OF THE INVENTION

The features and other details of the present invention will now more particularly be described as a step of the invention or as a combination of parts of the invention and will be described in the claims. It will be appreciated that certain embodiments of the invention are presented by way of illustration and not by way of limitation of the invention. The principles of the present invention may be utilized in various embodiments without departing from the scope of the invention.

The present invention generally relates to compositions comprising a fusion protein having an antigen that activates toll-like receptor 5 and has an isoelectric point greater than about 7.0, and a composition comprising a fusion protein in a composition for stimulating an immune response, such as a protective immune response, .

Lt; RTI ID = 0.0 &gt; TLR5 &lt; / RTI &gt; signaling to enhance the immunogenicity of the fusion protein, including the prasylin and the antigen. However, excess TLR5 signaling enhances inflammatory cytokine responses that can lead to in vivo systemic reactivity (e. G., Unwanted side effects such as heat, weight loss). The fusion protein comprising prazoline activates TLR5 signaling to maintain an isoelectric point that is less than the threshold of TLR5 signaling resulting in an adaptive immune response to antigens of greater than about 7.0 simultaneously resulting in unacceptable response.

Achieving a maximal TLR5 activity (rabbit model) associated with a good resistant composition comprising a minimal TLR5 activity (mouse model) and a fusion protein of Praseline for use in a vaccine required for the fusion protein comprising prazoline to become immunogenic Mouse and rabbit models were developed as described herein. In the mouse TLR5 activity model, if the mice are immunized with about 1 [mu] g fusion protein, the fusion protein will be at least about 32 pg / ml IL6 in the serum and about 80 pg / ml &lt; / RTI &gt; of TNF. In a rabbit model, a food consumption level exceeding about one standard deviation of the average of the buffer control was induced, body temperature was increased to about three standard deviations above the mean of the control, and the difference was greater than about 10 standard deviations from the average of the buffer control The capacity to increase C-reactive protein (CRP) is likely to be reactive in humans (e. G., With negative undesirable side effects). The dose ranges in which the compositions of the present invention are considered useful as vaccines remain non-reactive in the rabbit model and are described as "safety window ". The dosage ranges in which the compositions of the present invention are deemed useful as vaccines remain immunogenic but remain non-reactive in preclinical and clinical models and are described as "therapeutic window &quot;. The fusion protein achieves a suitable acceptable drug concentration for use in the method for stimulating protective immunity by adequately balancing the activation of the TLR5 signaling and the adaptive immune response to the antigen.

Fragmentel fused to an antigen at the carboxy-terminus of the full-length flazelin or flazelin that is not fused to any antigen has the narrowest safe drug concentration used in the composition to stimulate the immune response in the subject, Lt; RTI ID = 0.0 &gt; TLR5 &lt; / RTI &gt; signaling response. Antigens fused to the R3 construct of Praseline (US Application No .: 12 / 905,584) where the domain 3 of the prazoline is completely replaced by the antigen and the isoelectric point of less than about 7.0 have a broader safety drug concentration, Is considered to be due to the ability of the antigen to sterically hinder the binding of the protein, thus becoming a "partial agonist &quot;. The partial agonist activity of the R3 prazoline fusion protein is described in A / Puerto Rico / 08/34 and A / California / 07/09 (Taylor, et al., Vaccine 30: 5761-5769 have.

 There is sufficient partial TLR5 agonist activity on the fusion protein comprising prazoline to generate an immune response to the antigen component. As described herein, a sulcus having an isoelectric point greater than about 7.0 when fused to the R3 and R32x constructs of the praxelin induces reduced TLR5 signaling (reduced stimulation of the adaptive immune response) in the TLR5 active mouse model, It is therefore poor immunogenicity. Antigens with an isoelectric point greater than about 7.0 can induce intramolecular interactions between negatively charged prasuglene and the antigen. (E.g., about 7.0, about 7.5, about 8.0, about 8.5, about 9.0, about 9.5, about 10.0, about 10.5, about 11.0, about 11.5) from the domain 3 of the prazoline to at least one loop Is considered to preserve the ability of the fusion protein to activate TLR5 by the pregulin binding to TLR5 by forming an array that maximizes the spacing of the antigens from the TLR5 binding domain of Praseline.

In an embodiment, the invention includes a fusion protein comprising at least one antigen that is fused to at least one loop of domain 3 of flazelin and flazoline and has an isoelectric point greater than about 7.0. The fusion protein of the present invention activates toll-like receptor 5. In an embodiment, the antigen of the fusion protein of the invention used in the method of the invention has an isoelectric point of greater than about 7.5.

In another embodiment, the fusion protein used in the method of the invention and the antigen of the fusion protein of the invention have an isoelectric point of greater than about 8.0.

In yet another embodiment, the fusion protein used in the method of the invention and the antigen of the fusion protein of the invention have an isoelectric point of greater than about 8.5.

In a further embodiment, the fusion protein used in the method of the invention and the antigen of the fusion protein of the invention have an isoelectric point of greater than about 9.0.

In yet another embodiment, the fusion protein used in the method of the invention and the antigen of the fusion protein of the invention have an isoelectric point of greater than about 9.5.

In a further embodiment, the fusion protein used in the method of the invention and the antigen of the fusion protein of the invention have an isoelectric point of greater than about 10.0.

In another embodiment, the fusion protein used in the method of the invention and the antigen of the fusion protein of the invention have an isoelectric point of greater than about 10.5.

In yet another embodiment, the fusion protein used in the methods of the invention and the antigen of the fusion protein of the invention have an isoelectric point of greater than about 11.0.

Fusion of antigens to the loop of domain 3 of prasugin essentially maintains the domain 3 of praslin as its tertiary structure. As used herein, the phrase "essentially maintaining the domain 3 of prazoline in its tertiary structure" indicates that it maintains the tertiary structure of domain 3 of prazoline, which is responsible for activating TLR5 and evaluating the protective immunity Can be evaluated by well-established in vivo and in vitro assays as described herein, known to those of skill in the art, including the ability of Jellyn.

As used herein, a "fusion protein" refers to a fusion protein comprising at least two distinct elements: a portion of prazoline or prazoline, and a portion of about 7.0, about 7.5, about 8.0, about 8.5, about 9.0, about 9.5, Refers to a protein produced from an antigen or a portion of an antigen having an isoelectric point of 7.0 or greater, including an antigen having an isoelectric point of at least one member selected from the group consisting of SEQ ID NOs: 10.5 and 11.0.

The fusion proteins of the present invention can be produced by chemical conjugation or by recombination using well established techniques. The recombinant fusion protein may be produced by operably linking a nucleic acid sequence encoding a fragment of praslin or prazoline comprising domain 3 to a nucleic acid sequence encoding an antigen, e. G., An antigen that is at least a portion of an influenza virus antigen. The fusion proteins of the invention may comprise, for example, one, two, three, four or five antigens fused to one, two, three, or four loops of domain 3 of one or more of the plasins have.

The isoelectric point (pI) of a protein is the pH at which a particular antigen does not carry a net charge. The isoelectric point of the antigen fused to prasugin may be at least one member selected from the group consisting of about 7.0, about 7.5, about 8.0, about 8.5, about 9.0, about 9.5, about 10.0, about 10.5, and about 11.0. In an embodiment, the pI of the antigen is greater than about 7.0. In yet another embodiment, the pI of the antigen is greater than about 7.5. In a further embodiment, the pI of the antigen is greater than about 8.0. In yet another embodiment, the pI of the antigen is greater than about 8.5. In yet another embodiment, the pI of the antigen is greater than about 9.0. In a further embodiment, the pI of the antigen is greater than about 9.5. In yet another embodiment, the pI of the antigen is greater than about 10.0. In yet another embodiment, the pI of the antigen is greater than about 10.5. In yet another embodiment, the pI of the antigen is greater than about 11.0.

Among the fusion proteins of the present invention, Pradulin is S. typhimurium prazoline selected from the group consisting of S. typhimurium prazoline (UniProt accession no. P06179 or P52616), such as SEQ ID NO: 1 and 2; E. coli pravastatin (UniProt Accession No. AOPCV8), such as, for example, SEQ ID NO: 3; P. Ke rugi labor (P. aeruginosa) PRA jelrin (UniProt accession number P72151), for example, SEQ ID NO: 4; Aquifex aeolicus VF5 Praseline (UniProt Accession No. O67803), such as SEQ ID NO: 5; Helicobacter pylori (Helicobacter pylori) J99 plastic jelrin A (UniProt accession number P0A052), for example, SEQ ID NO: 6; And Legionella pneumophila pravastatin (UniProt Accession No. Q48824), such as SEQ ID NO: 7.

The fraxelin used in the fusion protein of the present invention includes at least a portion of the carboxy-domain 0 or a portion of the amino-domain 0, such as about 5, about 10, about 14, about 15 and about 20 of the carboxy- At least one member selected from the group consisting of amino acids or a part of the amino-domain 0 may be absent. As shown in Fig. 14, Prazoline comprises carboxy-domain 0, carboxy-domain 1, carboxy-domain 2, domain 3, amino-domain 2, amino-domain 1 and amino-domain 0. Where prazoline is assumed to be its tertiary structure, domains 2 and 3 form a junction where prazoline is formed in which the majority of the carboxy-amino acid of the carboxy-domain 0 of the prazoline is the amino of most of the amino-domain 0 of the prazoline - folded to be adjacent to amino acids. A crystallographic study of prazoline confirmed the secondary and tertiary structure of S. typhimurium FliC prazoline (SEQ ID NO: 1) (PDB code: 1UCU).

The phrase "loop of domain 3 of prazoline" as used herein refers to an amino acid stretch in domain 3 of prazoline, which itself has a secondary structure (e.g., beta-sheet, alpha -helix) But is located on the side of the stretch adjacent to the amino acid of domain 3, including the secondary structure such as? -Sheet,? -Helix. The loop of domain 3 of the praxelin may be about 2, about 3, about 4, about 5, about 6, about 7, and about 5 to about 30 amino acids in length. Exemplary loops of domain 3 of S. typhimurium prolazzin (SEQ ID NO: 1) are depicted in Figures 14, 29 and 30, wherein "D3I-ol", "D3I-il", "D3I quot; -cl "and" D3I-sl ".

Prazoline (FljB) from Salmonella typhimurium is depicted as SEQ ID NO: 2. Domain 3 of Salmonella typhimurium protozillin is amino acid residue 191 to amino acid residue 291 of SEQ ID NO: 2. Prazoline from E. coli (UniProt Accession No. AOPCV8) is depicted as SEQ ID NO: 3. Domain 3 of E. coli pregulin of SEQ ID NO: 3 is predicted from amino acid residue 191 to amino acid residue 283 of SEQ ID NO: 3. P. auriginosa prazoline (UniProt Accession No. P72151) is depicted as SEQ ID NO: 4, and domain 3 is predicted as an amino acid residue. Prasugene from aciphexa aeroxus VF5 (UniProt Accession No. O67803) is depicted as SEQ ID NO: 5. Domain 3 of aciphexa aequosusprazelin is predicted from amino acid residue 197 to amino acid residue 302 of SEQ ID NO: 5. Prazoline A from Helicobacter pylori J99 (UniProt Accession No. P0A052) is depicted as SEQ ID NO: 6. Domain 3 of Helicobacter pylori J99 of SEQ ID NO: 6 is predicted from amino acid residue 189 to amino acid residue 283 of SEQ ID NO: 6. Prazoline from Legionella pneumophila (UniProt accession number Q48824) is depicted as SEQ ID NO: 7. Domain 3 of Legionella pneumophila prasuglain of SEQ ID NO: 7 is predicted from amino acid residue 189 to amino acid residue 283 of SEQ ID NO: 7.

X-ray crystallographic analysis of Salmonella typhimurium FliC prazoline (SEQ ID NO: 1) shows that domain 3 of Praslin contains six loops (Figure 29). The loop of domain 3 of Salmonella typhimurium protoplastin SEQ ID NO: 1 comprises amino acid residues 211-212 (loop 1); Amino acid residues 217 to 219 (loop 2); Amino acid residues 223 to 229 (loop 3); Amino acid residues 237-242 (loop 4); Amino acid residues 250 to 255 (loop 5) and amino acid residues 259 to 275 (loop 6).

Figure 29 identifies the predicted loop (gray) of domain 3 of Salmonella typhimurium FljB prasuglene (SEQ ID NO: 2) and identifies the predicted loop (gray) of Salmonella typhimurium FljB prasugrel (SEQ ID NO: And the position of the sequence is compared. The dark gray arrow depicts the secondary structure of domain 3 of S. typhimurium FliC, e.g., beta -sheet and alpha -helices.

Figure 30 shows the potential fusion sites of antigens with Salmonella typhimurium FljB prasugin (SEQ ID NO: 2), boundaries of domains 0, 1, 2 and 3, and an isoelectric point of greater than about 7.0 in the loop of the flagellin domain 3 . In an embodiment, the fusion site of an antigen with an isoelectric point greater than about 7.0 is referred to as D3I-i1 (also referred to as "D3Ins-i1") amino acid residues 259-260 of SEQ ID NO: 2 in loop 5 of domain 3, (See FIG. 29). In another embodiment, the fusion site of an antigen with an isoelectric point greater than about 7.0 is referred to as D3I-o1 (also referred to as "D3Ins-o1") at amino acid residues 277-278 of SEQ ID NO: 2 in loop 6 of domain 3 (See FIG. 29).

In another embodiment, the D3I-o1 site of the antigen fusion with an isoelectric point greater than about 7.0 is amino acid residues 274-275 of SEQ ID NO: 4 in predictor loop 6 of domain 3. In yet another embodiment, the D3I-o1 site of the antigen fusion with an isoelectric point greater than about 7.0 is amino acid residues 274-275 of SEQ ID NO: 5 in predictor loop 6 of domain 3.

In another embodiment, the D3I-i1 site of the antigen fusion with an isoelectric point greater than about 7.0 is amino acid residues 258 to 259 of SEQ ID NO: 4 in the predictive loop 5 of domain 3. In yet another embodiment, the D3I-o1 site of the antigen fusion with an isoelectric point greater than about 7.0 is amino acid residues 260-261 of SEQ ID NO: 5 in the predictive loop 5 of domain 3.

The antigen can be fused to domain 3 of the prazoline to produce a construct called D3I-o1 and D3I-i1. As used herein, "D3I-o1" refers to an insertion (domain 3) of the domain 3 on the outer ( o ) or concave surface of the flagellin such as loop 6 of SEQ ID NO: 2 or SEQ ID NO: shows an insertion part (D omain 3 I nsertion)) . As used herein, "D3I-i1" refers to the loop of domain 3 on the interior ( i ) or convex surface of the flagellin, such as loop 3 of SEQ ID NO: 2 and SEQ ID NO: Part of the praselin to be regarded as concave and convex surfaces of the praglet and the tertiary structure of the praglet are described, for example, in Samatey, et al., Nature 410: 331-337 (2001).

In the insertion of an antigen (D3I-cl) into the loop of domain 3 of prasuglene, designation "c" refers to the "side-way" part of domain 3 (FIG. 14).

For antigen insertion into the loop of domain 3 (D3I-s1) of prazoline, the designation "s" refers to the "tip" of domain 3 of the prazoline (FIG. 14).

Exemplary fusion proteins of the invention are shown in SEQ ID NO: 126, 128-130, 151, 157-193.

The conjugation of the antigen and the fragment of the fusion protein of the present invention leads to a unique amino acid sequence. In a fusion protein used in the method of the present invention for treating a human, when such a unique amino acid sequence shares homology with a known human protein at the junction of the fusion of the flagellin element and the antigenic element, Or to induce an unwanted immune response to a portion of a human protein. Upon selection of the insertion site of the prazoline (e.g., the carboxy- or amino-terminal proximal portion of domain 2 of R3 construct, loop of domain 3), the unique amino acid sequence to be generated by fusion of the antigen to prazoline It is evaluated for its potential to cause unwanted immune responses. In the evaluation, probes of about 10 to about 12 amino acids in length, including a praslin / antigen junction, are used to probe databases of known human genomic sequences. If homology is found for an amino acid stretch of greater than about 5 amino acids, the junction sequence is modified with, for example, amino acid substitutions of 1, 2, 3, 4, 5, or 6 amino acids to reduce homology. The preferred order of amino acids for use in the modification is serine, threonine, alanine, and glycine. Generally, a single amino acid substitution is sufficient to alter homology. For example, see SEQ ID NO: 283 in the native FljB sequence of the domain 3 member. For example, in the R3 construct of Praseline, Arg405 of SEQ ID NO: 283 may be changed to an alanine residue to produce SEQ ID NO: 284. Alternatively, Ala191 of SEQ ID NO: 283 may be changed to a serine residue, Arg405 of SEQ ID NO: 283 may be changed to alanine, and the serine residue may be replaced with an altered alanine residue (i. E., The most carboxy- ) To generate SEQ ID NO: 285. An exemplary fusion protein having an altered amino acid residue at the junction of the fusion of antigen and prasylin is SEQ ID NO: 268, wherein the HA1-2 portion of SEQ ID NO: 286 is fused to the flazelin of SEQ ID NO: 285 do. In SEQ ID NO: 268, the junction of the fusion of antigen and prazoline is Ala190 and Gly191; Ser413 and Ser414; Ala628 and Ser629 and Gly630.

In embodiments, the fraxelin used in the fusion protein of the invention lacks at least one member selected from the group consisting of at least a portion of carboxy-domain 0 and at least a portion of amino-domain 0.

In another embodiment, at least one additional antigen is fused to the prazoline at a site that is separate from the antigen fusion to the loop of domain 3 of the prazoline. This additional antigen may be an antigen similar to an antigen fused to at least one loop of domain 3 of the flagellin. Alternatively, the additional antigen may be an antigen (also referred to herein as "distinct") antigen that differs from the antigen fused to at least one loop of domain 3 of the flagellin. For example, at least a portion of the influenza hemagglutinin antigen, such as the HA1-1 or HA1-2 portion, is linked to the loop of domain 3 of the praxelin (e. G., Amino acid 277 of loop 3 of SEQ ID NO: 278), and another part of the influenza hemagglutinin antigen, e. G., HA1-1L, may be fused to a different loop of domain 3, e. G., Between amino acids 259 and 260 of loop 5 of SEQ ID NO: .

In another embodiment, the insertion site of the antigen in the loop of domain 3 of Praseline is separated from the insertion site identified in Figures 14, 29 and 30 to amino-domain 2 of the pregulin or 1, 2, About 3, about 4, about 5, about 6, about 7, about 8, about 9, about 10 amino acids. For example, with respect to SEQ ID NO: 2, the loop of domain 3 to which the antigen is fused may be amino acid residues 277 and 278 (e.g., D3I-o1) (Figure 30). Alternatively, fusion of the antigen may occur at amino acids 266-282 of SEQ ID NO: 2.

Similarly, with respect to SEQ ID NO: 2, the loop of domain 3 in which the antigen is fused is amino acid residues 259-260 (D3I-i1) or amino acid residues 260-261. The insertion site of the loop of domain 3 in the D3I-i1 fusion protein of SEQ ID NO: 2 is amino acid residues 190-191 or amino acid residues 291-292.

In another embodiment, about 2 to about 4 amino acid residues in the loop of domain 3 can be deleted prior to fusion with an antigen having an isoelectric point greater than about 7.0. The deletion will be designed so that the adjacent secondary structure of the prazoline is not destroyed. This deletion in at least one loop of domain 3 of prazoline can be used when prazoline is fused to a relatively large antigen.

In a preferred embodiment, the flagellin for use in the fusion protein is a flagellin comprising at least one member selected from the group consisting of SEQ ID NO: 1-7. The antigen is fused to amino acid residue 191 to amino acid residue 285 of SEQ ID NO: 1, which is in the loop of domain 3 of the praxelin.

In certain embodiments, the antigen fused to the loop of domain 3 of the flagellin is an influenza virus antigen, particularly an influenza B virus antigen.

In another embodiment, the influenza virus antigen is at least a portion of the influenza A antigen subtype (H3, H7, H5 or H9). The influenza A antigen subtype may be at least one member selected from the group consisting of H3, H5, H7 and H9. Additional influenza A antigen subtypes may be at least one member selected from the group consisting of H1 and H2 subtypes (H1 subtype or H2 subtype).

In certain embodiments, the influenza virus antigen is part of a hemagglutinin antigen, including at least a portion of a spherical head of hemagglutinin, particularly a hemagglutinin antigen. Some of the influenza virus hemagglutinin used in the fusion proteins of the present invention preferably comprise at least a portion of a spherical head of hemagglutinin comprising a sialic acid binding site. A portion of the spherical head of the hemagglutinin comprises at least one ß-sheet at the bottom of the spherical head, which causes the spherical head to essentially maintain its tertiary structure.

The phrase "sialic acid binding site " as used herein in connection with a portion of a protein from a naturally occurring virus hemagglutinin refers to a portion of an influenza virus hemagglutinin having the ability to interact with a sialic acid residue do. "Sialic acid binding site" is also referred to herein as "sialic acid binding domain ".

As used herein, "at least a portion" refers to an antigen or any portion of the antigen or prazoline that is less than the total of the prazoline.

The phrase " globular head " as used herein refers to a portion of a protein of influenza virus hemagglutinin comprising a receptor or sialic acid binding domain. The "conceptual head" is also referred to herein as a "concept domain ". Spherical heads of viral hemagglutinin proteins are described, for example, in Wilson I. A., et al. Nature 289: 366-373 (1981); Chen, J., et al., Cell 95: 409-417 (1998); Ha Y., et al., The EMBO Journal 21: 865-875 (2002); Russell, R. J., et al., Virology 325: 287-296 (2004); and Cox, N. J., et al., In: Toply and Wilson's Microbiology and Microbial Infections, eds. BWJ Mathy, et al., Vol. 1 (9th ed.) New York, NY, Oxford Univ. Press, Ch. 32, p. 634 (1998)). &Lt; / RTI &gt; The bulbous head of the influenza virus hemagglutinin is an element of the HA1 subunit of the influenza virus hemagglutinin. In addition to the receptor binding domain, spherical heads are described, for example, in Ha, Y., et al. The &lt; / RTI &gt; EMBO Journal 21: 865-875 (2002).

The phrase "the spherical head essentially retaining its tertiary structure" as used herein means mimicking the tertiary structure of the spherical head in the naturally occurring influenza virus hemagglutinin by maintaining the tertiary structure of the spherical head , Which can be assessed by viral neutralization in vitro assays as described herein or the ability to generate an immune response sufficient to stimulate a protective immune response in a subject in vivo.

Influenza viruses are single-stranded RNA viruses belonging to the virus family Orthomyxoviridae . Influenza viruses are divided into three types (A, B, C), which are determined by antigenic differences in the ribonucleic acid protein (RNP) and matrix (M) antigens of the virus. Influenza A virus naturally infects humans and a number of other mammalian species, including humans and pigs and horses, and a wide variety of avian species, resulting in epidemics and pandemics in the human population. Influenza B virus appears to naturally infect only humans and seals, and can cause epidemics in humans. Influenza C viruses have been isolated from humans and pigs, but generally do not occur as epidemics, and generally result in mild illness in humans.

Mature influenza virions are enveloped in a polymorphic structure ranging from about 80 to about 120 nm in diameter. The single-stranded RNA genome is closely related to the helical nuclear protein and is present in a separate segment of seven (influenza C) or eight (influenza A and B) ribonucleic acid proteins (RNPs) It must exist for successful replication. The segmented genome is encapsulated within the outer lipid protein envelope. Matrix protein 1 (referred to herein as MP1 or "Ml") is lined inside the outer lipid protein shell and bound to RNP.

Hemagglutinin (HA) is a surface glycoprotein on a virus (e. G., Influenza virus), which binds to N-acetylneuraminic acid (NeuNAc; also referred to herein as "sialic acid & And subsequently contribute to the fusion of the virus and the host membrane. HA has been named by his ability to clothe or stagger red blood cells. Influenza HA consists of three monomer (HA0) subunits. HA performs two important functions during the infection process: binding to cell surface sialyl oligosaccharide receptors and fusion of viruses and host cell membranes. After binding of HA to the plasma membrane of the host cell, the host cell membrane swallows the virus in the endosome, acidifies the interior of the endosome and transfers it to the lysosomes in the host cell, thereby attempting to break down the contents of the endosome. However, the acidic environment of lysosomes destabilizes HA, resulting in a partial superposition loosening of HAO, which exposes protease-sensitive sites (mature cleavage sites) that are cleaved by the host protease to form HA1 and HA2 subunits, They are linked by a single disulfide bond (Wiley, DC, et al., Annu. Rev. Biochem. 56: 365-394 (1987)). Cleavage occurs at a specific amino acid residue and produces a hydrophobic amino terminus for the HA2 subunit. The hydrophobic end of HA2 mediates the fusion between the viral envelope and the endosomal membrane of the host cell, releasing the contents of the virion into the cytoplasm of the cell (a process known as decohesion). Thus, cleavage of HA polypeptides is necessary for infectivity.

The crystal structure of several viral hemagglutinins was measured (see, for example, Wilson, IA, et al., Nature 289: 366-373 (1981); Chen, J., et al., Cell 95: Russell, RJ, et al., Virology 325: 287-296 (2004); and Cox, NJ (1998); Ha, Y., et al., The EMBO Journal 21: 865-875 , et al., In: Toply and Wilson's Microbiology and Microbial Infections, eds. BWJ Mathy, et al., Vol 1 (9th ed.), New York, NY, Oxford Univ. Press, 1998)). The X-ray crystallographic structure shows that HA is superimposed on two structural elements or domain-globular heads and fiber stems (e.g., see FIG. 1). The spherical head comprises HA1 comprising HA1 moiety (also referred to as "receptor binding site or domain" or "sialic acid binding site or domain") that binds to sialic acid, and antiparallel β-sheet. The fiber stem is closer to the viral membrane and comprises HA1 moiety and HA2 subunit that contain the cleavage site between HA1 and HA2.

There are 17 known influenza A HA subtypes (H1-H17) that share about 40 to about 60% sequence identity (Tong, et al., Proc. Natl. Acad. Sci., 109: 4269-4274 )). Influenza viruses containing all 17 HA subtypes have been shown to be effective against influenza viruses such as, for example, algae species H5, H7 and H9, horses H3 and H7, seals H3, H4 and H7, whales H1 and H13, (H1, H3, and H9). The subtypes of influenza A virus are generally named according to the specific antigenic determinant of HA (H, 17 major types) and neuraminidase (N, about 9 major types). For example, the subtype is influenza A (H2N1), A (H3N2), A (H5N1), A (H7N2), A (H9N2) H0) and A (H7N9). In the last century, three subtypes of influenza A resulted in type illness: H1 in 1918, 1977 and 2007; H2 in 1957 and H3 in 1968. In 1997, the H5 bird virus and the H9 virus in 1999 caused respiratory disease in Hong Kong.

HA from influenza type B has been isolated from humans and seals and is not divided into subtypes, while influenza type B viruses are characterized by Lineage of two antigens, namely, Yamagata and Victoria. Influenza type B virus strains from both Yamagata and Victoria Lineage typically co-circulate. The composition used in the influenza vaccine may comprise, in addition to the two A strains, four antigens comprising both of the circulating strains B (i. E., "Safflower vaccine"). Similar to influenza A HA, X-ray crystallography studies of influenza B HA revealed four major antigenic regions located near the receptor binding site present in the bulbous head of influenza B HA (Wang, Q., et al., J Virol., March: 3011-3020 (2008)).

An influenza-infected host initiates an antibody response to the spherical head of HA to protect its host from subsequent infection with the virus of the same strain by blocking the interaction between HA and the host cell, i.e., neutralizing viral infectivity. Due to its low accuracy and high replication rate of influenza RNA, the virus constantly experiences small head loss in the HA gene, although the bulbous head structure and host cell interactions are preserved, but the offspring virus can escape immune surveillance. This point mutation is referred to as "antigenic drift ". Also, if a single host is simultaneously infected with two different strains of influenza A, the new subtype virus can occur as a result of RNA segmentation or gene exchange or rearrangement between different influenza A virus strains. Viruses resulting from rearrangements cause the human immune system to experience new antigens, which generally result in high morbidity and mortality. This type of intense antigen exchange is known as "antigenic shift. &Quot; Since Type B influenza virus circulates almost exclusively in humans, these viruses can not be rearranged with animal strains, and therefore only antigenic urine is exchanged by.

Immunity to HA can reduce the severity of the disease in the event of infection and the possibility of infection. HA is an important antigen target, and the efficiency of the vaccine depends on the antigen match between the vaccine strain and the circulating strain. Because hemagglutinin protein easily produces antigenic feces and antigen urine to avoid host immune defense, traditional vaccines should be based on current circulating influenza strains and should be updated annually. Updating an influenza vaccine every year is not only costly, but also requires a significant amount of production time and production infrastructure. Vaccine compositions based on constant regions of virus can provide a wide range of cross-reactive protection.

Hemagglutinin forms a trimer on the surface of influenza virus and infected cells. The monomeric subunits of the trimer are depicted in Figure 1 and include HA1 subunit (membrane proximal spherical head) and HA2 subunit (membrane proximal "stem"). Portions of HA for use in the compositions of the present inventors may comprise at least a portion of a spherical head, which includes a cell surface receptor binding site and most neutralizing antibody epitopes. A portion of the HA called HA1-1 and HA1-2 subunits fused to prazoline (R3 and R32X constructs of Prazoline, see for example US patent application Ser. No. 12 / 905,584) (See, for example, U.S. Patent No. 8,420,102). The HA1-1 and HA1-2 portions of the HA include a portion of the spherical head, and the amino acid length and secondary structure are different. The HA1-1 and HA1-2 portions include at least one β-strand at the bottom of at least a portion of the spherical head of the HA and a portion of the spherical head that maintains a portion of the spherical head in its tertiary structure.

The HA1-1 and HA1-2 portions of certain influenza virus antigens, when fused to the R3 or R32x format (or "R3 constructs" or "R32x constructs" (See, for example, U.S. Patent No. 8,420,102). The fusion protein fused to prazoline in the region of prazoline, which contains prazoline lacking the entire domain 3 and the HA antigen was domain 3, is referred to as "R3 fusion protein ". The R32x fusion protein (also referred to as "R3.2x") is an R3 fusion protein comprising a secondary antigen fused to the carboxy-terminal amino acid of the carboxy-domain of the prazoline, (See, for example, U.S. Patent Application No. 12 / 905,584). For example, the HA1-1 portion can be fused to the region of the pregulin, which was domain 3, and the HA1-2 portion can be fused to the carboxy-terminal amino acid of the pregulin to form the R32x fusion protein.

In contrast, in certain strains of influenza A, the R3 and R3.2x fusion proteins, including portions of influenza B HA, exhibit poor immunogenicity as shown herein. For example, Yamagata Lineage strain B / Florida / 4/2006 or R3 format (HL169, SEQ ID NO: 122) fused to the flagellin of the R2 format (HL118, SEQ ID NO: (SEQ ID NO: 147) or the Victoria Lineage strain B / Brisbane / 60/2008 fused to the flagellin of the R32X format (HL171, SEQ ID NO: 288), the HA1-2 portion of SEQ ID NO: 264 ) Failed to induce a measurable level of hemagglutination inhibition (HAI) activity, a standard measure of protective immunity against influenza viruses. Every year, new polyvalent blends of compositions for use as vaccines are developed as therapeutic agents to prevent and manage diseases associated with viral influenza infection. For example, the antiretroviral vaccine (TIV) therapeutic agent contains two different inactivated influenza type A strains and one inactivated influenza type B strain (for example, FLUVIRIN ^® ). SAGA VACCINE (QIV) TREATMENT For example, the FLUZONE ^® vaccine is available, which contains two different inactivated influenza type A strains and two inactivated influenza B strains. Thus, there is a need to develop new and effective fusion proteins that can be incorporated into polyvalent compositions and target influenza B.

Influenza virus antigens fused to at least one loop of domain 3 of prazoline may be part of an influenza B virus antigen, e.g., a moiety referred to herein as "HA1-1", "HA1-2", and "HA1-1L" . Influenza virus hemagglutinin antigens, such as the HA1-1, HA1-2 and HA1-1L portions of influenza hemagglutinin can be used in methods for treating or preventing seasonal and pandemic influenza in a subject.

Influenza virus antigens For example, "part" as used herein in reference to influenza virus hemagglutinin antigens refers to any portion of the influenza virus hemagglutinin that is less than all of the influenza virus hemagglutinin.

In some embodiments, a portion of the influenza virus hemagglutinin (HA) antigen is part of the spherical head of HA. In another embodiment, a portion of the influenza virus HA is the whole spherical head.

As used herein, "HA1-1" includes, at the bottom of the molecule, at least about one ß-sandwich (including a substrate binding site) comprising at least about 2 ß-sheets, at least about 2 to about 3 short a Refers to a protein portion of a virus hemagglutinin comprising at least one small ß-sheet and at least one additional small ß-sandwich, and at least about 4 disulfide bonds. The ß-sandwich comprising the substrate binding site of HAl-1 comprises at least about 4 ß-strands as a top sheet and at least about 3 to about 4 ß-strands as a bottom sheet. At least about one a-helix of the HAl-1 moiety is located on the side of the ß-sandwich that includes the substrate binding site and at least about 1 to about 2 is located at the bottom of the ß-sandwich that includes the substrate binding site. The small ß-sandwich of HAl-1 has at least about 2 to about 3 ß-strands in each ß-sheet; Or from about 3 to about 4 beta-strands. Exemplary HA1-1 protein portions include SEQ ID NOs: 8-44. In certain embodiments, the HA1-1 portion of the HA comprises a portion of the bulbous head of the HA having the ß-sandwich and the ß-sheet of spherical head bottom essentially retaining the spherical head in its tertiary structure.

As used herein, "HA1-2" includes, at the molecular bottom, at least one ß-sandwich comprising a substrate binding site, at least about 2 to about 3 short a-helix, at least about one small ß- Quot; refers to a protein portion of a virus hemagglutinin that comprises at least about two disulfide bonds. The ß-strand of the virus hemagglutinin may comprise from about 2 to about 15 amino acids. The small ß-strand contains about 2 amino acids; Or from about 2 to about 3 amino acids; Or about 2 to 4 amino acids or about 2 to about 5 amino acids. The small ß-sheet comprises about 2 to about 3 ß-strands; Or about 3 to about 4 b-strands. The ß-sandwich comprising the substrate binding site of HAI-2 may additionally comprise at least about four ß-strands as a top sheet and at least about 3 to about 4 ß-strands as a bottom sheet. At least about one a-helix of the HA1-2 moiety is located on the side of the beta-sandwich comprising the substrate binding site and at least about 1 to about 2 of the moiety is located at the bottom of the beta-sandwich comprising the substrate binding moiety. Exemplary HA1-2 protein portions include SEQ ID NOs: 45-97 and 287. In certain embodiments, the HA1-2 portion of the HA comprises a b-sheet at the bottom of a portion of the spherical head of the hemagglutinin.

In another embodiment, a portion of influenza virus hemagglutinin fused to at least one loop of domain 3 of all or at least a portion of the flagellin comprises at least two [beta] -sheets and at least one [beta] -sheet comprises At least about 2 to about 3 a-helix and at least about 4, at least about 5, at least about 5, at least about 5, at least about 5, at least about 6, (Having a substrate binding site) of a spherical head of hemagglutinin having at least about 6, at least about 7, or at least about 8 disulfide bonds, and optionally, at least one a- - optionally located at the bottom of the? -Sandwich of the substrate binding site and optionally at least one or two? -Helices located at the bottom of the spherical head The β-sheet of the spherical head comprises at least two to three β-strands or three to four β-strands at each β-sheet of the β-sandwich, the β-sandwich comprises at least 3 β-strands in each β-sheet of the β-strand or β-sandwich and, alternatively, the β-sandwich of the substrate binding site comprises at least 4 β-strands in the top sheet of β- beta-sandwich comprises at least 3 to 4 beta strands in the bottom sheet; Alternatively, the membrane fusion domain is absent; Lacking the transmembrane domain, and lacking the cytoplasmic domain.

In yet another embodiment, the influenza virus hemagglutinin portion fused to at least one loop of domain 3 of all or at least a portion of the prazoline comprises a portion of a spherical head of hemagglutinin having a substrate binding site Which comprises at least about a beta sandwich and comprises at least one beta sheet that allows the spherical head portion to inherently maintain its tertiary structure at the bottom of the bulbous head portion and comprises at least about 2 to about 3 (or at least about 3 disulfide bonds or at least about 4 disulfide bonds, or at least about 5 disulfide bonds, or at least about 6 disulfide bonds, or at least about 7 disulfide bonds) Alternatively, at least one a-helix is located on the side of the [beta] -sandwich of the substrate binding site , Optionally, at least one or two α- helix is located on the bottom of the β- sandwich the substrate binding site; Optionally, the? -Sandwich of the substrate binding site comprises at least four? -Fabrics as the top sheet of? -Sandwich and at least three to four? -Fabrics as the bottom sheet of? -Sandwich, and optionally the membrane fusion domain Lack; Lacking the transmembrane domain, and lacking the cytoplasmic domain.

A single polypeptide may represent several types of secondary structures. Without any stabilization interaction, the polypeptide may be in the form of a random-coil. However, secondary structures such as alpha (alpha) -helix and beta (beta) -strands can stabilize proteins or portions of proteins. The side association of the? -sheets forms a? -sheet (also referred to herein as a "? -shaped structure"). The secondary structure may be located on the surface of an antigen (e. G., A portion of a viral hemagglutinin). The tertiary structure of the protein is a three-dimensional array of amino acid residues. For example, compared to a secondary structure stabilized by a hydrogen bond, a-helix, b-strand, the tertiary structure is induced by the hydrophobic interaction between the non-polar side chains of a part of the antigen, such as influenza virus hemoglobin . The hydrophobic interaction keeps the helix strand of the random coil in a dense internal framework. The size and shape of the protein may be dependent on the number, size and arrangement of secondary structures as well as its major amino acid sequence.

A portion of the influenza virus hemagglutinin for fusion to at least one loop of domain 3 of prasuglins comprises at least a portion of a globular head having a secondary structure at the bottom of the spherical head that causes the spherical head to remain essentially in its tertiary structure . This secondary structure comprises at least one ß-sheet; At least one ß-sheet and at least one ß-sandwich; At least one ß-sheet, at least one ß-sandwich and at least two ß-strands.

Some of the hemagglutinin used in the compositions of the present invention that are fused to at least one loop of domain 3 of prasugin may lack the transmembrane domain and the cytoplasmic domain. Some of the hemagglutinin used in the composition of the present invention may further lack at least a portion of the HA2 subunit or the HA2 subunit of hemagglutidine.

An antigen having an isoelectric point greater than about 7.0 may be fused to at least one loop of domain 3 of the prazoline to form a fusion protein of the invention. A loop of domain 3 that can be characterized as an "extended region" comprises about 50 to about 100 amino acids, from about 100 to about 250 amino acids and from about 250 amino acids to about 500 amino acids Including about 50 amino acids, about 100 amino acids, about 150 amino acids, about 200 amino acids, about 250 amino acids, about 300 amino acids, about 350 amino acids, about 400 amino acids, about 450 amino acids, An amino acid insert of about 500 amino acids in length can be accommodated. For example, the fusion protein of SEQ ID NO: 126 (HL772) comprises a portion of influenza B / WI1 having a length of 249 amino acids; The fusion protein of SEQ ID NO: 128 (HL657) comprises a portion of influenza B / BR60 having a length of 250 amino acids; The fusion protein of SEQ ID NO: 129 (HL775) comprises a portion of influenza A / PE16 having a length of 275 amino acids; The fusion protein of SEQ ID NO: 130 (HL1018) contains a portion of influenza A / AH1 having a length of 282 amino acids.

Antigens having an isoelectric point greater than about 7.0 include secondary structures such as at least one? -Sheet, at least one? -Sandwich, at least one? -Fold, and at least one? -Helic acid, When fused to the loop of domain 3, it maintains its tertiary structure in a dense array, thus minimizing the tertiary structure of the loop of domain 3.

There are at least 17 different HA antigens, and these different HA antigens are classified as subtypes and identified as HA1 to H17. H1, H2 and H3 are found in human influenza virus antigens. The hemagglutinin of the influenza virion is a trimer (three copies of the HA polypeptide). The cleavage site for the cell protease on the HA protein is located near the viral membrane. The non-cleaved form of hemagglutinin is referred to as HAO. After cleavage by a cell enzyme, two subunits of HA, specifically HA1 subunit and HA2 subunit, are generated. The two subunits are held together on the surface of the virus particle. The HA2 subunit generated by cleavage contains a sequence of a hydrophobic acid termed as a fusion peptide.

In a further embodiment, a portion of the hemagglutinin fused to at least one loop of domain 3 of flazoline, e. G. The HA1-2 portion of SEQ ID NO: 45-97, comprises at least one ß - Have a seat. In addition to at least one ß-sheet at the bottom of the portion of the spherical head, a portion of the hemagglutinin fused to at least one loop of domain 3 of the praslin is connected to at least one ß-sandwich at the bottom of the spherical head, , And at least two ß-strands at the bottom of the spherical head portion. Thus, a portion of the influenza virus hemagglutinin fused to at least one loop of domain 3 of the flagellin comprises at least one ß-sheet at the bottom of a portion of the bulbous head of the influenza virus hemagglutinin, at least one ß- Sandwich, and at least two ß-strands, referred to herein as the "HA1-1L" portion of hemagglutinin. Exemplary HA1-1L portions of HA are SEQ ID NOs: 98-121, 228 and 273-277.

The fusion protein of the present invention may comprise an amino acid linker between the loop of domain 3 of the flagellin and at least one of the amino-terminal or carboxy-terminal of the antigen. The amino acid linker may be about 1 to about 10 amino acids in length, such as about 2, about 3, about 4, about 5, about 8 or about 9 amino acids in length. Preferred amino acid residues will include amino acid residues with no side chains or amino acid residues with glycine, alanine or serine, including combinations of small side chains such as glycine, serine and alanine. For example, an amino acid residue of a linker of at least about 9 amino acids in length may be fused to the carboxy-terminus of the antigen (HL352) of SEQ ID NO: 125 in the fusion protein. Exemplary antigens fused to the linker are SEQ ID NOs: 46, 48, 50, 52, 54, 56, 58, 60, 62, 89, 91, 93-97, 228, 273-277. An amino acid residue comprising an amino acid linker may have an isoelectric point of from about 3 to about 7 and from about 4 to about 7. [ An amino acid linker may comprise 2, 3, 4 or 5 negatively charged amino acid residues, such as aspartic acid or glutamic acid. Exemplary amino acid linkers are described, for example, in PCT / US2012 / 000099 (WO 2012/115715), by Song, L. et al., And PCT / US2012 / 000367 (WO 2013/066365), by Song, L. et al. , et al. The negatively charged amino acids at or near the amino- or carboxy-terminus of the antigen at the fusion site to the loop of domain 3 (about 1, 2, 3, or 4 amino acids) are positively charged with positively charged It is believed that the undesired intramolecular interactions between charged antigens are diminished and the antigens are tethered at the fusion site. Amino acid linkers lack secondary structures such as a-helix and b-sheet.

In an embodiment, the linker is naturally occurring in the naturally occurring hemagglutinin and comprises HA (SEQ ID NO: 123) fused to the loop of domain 3, such as the nine amino acid residues of SEQ ID NO: 123 (E. G., HA1-1, HA1-2, HA1-1L), which comprises two negatively charged amino acid residues. For example, the fusion protein of SEQ ID NO: 154 (HL719, which is the R3 construct) contains a portion of the influenza B Wisconsin construct (HA1-2 of SEQ ID NO: 50) and two negatively charged residues (SEQ ID NO: 123) of the naturally occurring hemagglutinin. Exemplary antigens fused to the same linker are SEQ ID NOs: 46, 48, 52, 54, 56, 58, 60, 62, 89, 91, The fusion protein of SEQ ID NO: 152 (HL724, R3 construct) contains influenza B Wisconsin HA1-2 having nine amino acids of SEQ ID NO: 123 with additional three negatively charged amino acid residues in a portion of HA . Exemplary antigens fused with the same variant are SEQ ID NOs: 94-97.

The amino acid linker used to fuse the antigen into at least one loop of Domain 3 of Praseline includes about 1 to about 10 amino acids in length, such as about 2 amino acids, about 3 amino acids, about 4 amino acids, about 5 amino acids , About 6 amino acids, about 7 amino acids, about 8 amino acids, about 9 amino acids, and about 10 amino acids. Preferably, the amino acid linker comprises amino acid residues with or without small side chains such as glycine, alanine and serine. In certain embodiments, the amino acid linker to be fused to the carboxy-terminus of the loop of domain 3 of flazelin has an overall negative charge such as an isoelectric point of from about 2 to about 4.

In a further embodiment, the invention is a composition comprising at least three fusion proteins each activating toll-like receptor 5. The first fusion protein comprises a first influenza A virus hemagglutinin antigen fused to a portion of the first flazelin and having an isoelectric point of greater than about 6.0, such as an isoelectric point of from about 6.5 to about 7.0. The second fusion protein comprises a second influenza A virus hemagglutinin antigen fused to a portion of the second flazelin, and the antigen is distinguishable from the first influenza A virus hemagglutinin antigen Has an isoelectric point of greater than about 7.0, such as about 7.5 to about 8.5, about 7.8, about 8.0, about 8.5, about 9.0, and about 9.5. The third fusion protein is fused to at least one loop of domain 3 of the third plasine and the third fragment and has an isoelectric point of greater than about 8.0, such as from about 8.0 to about 10.0, about 8.5, about 9.0, about 9.5, Lt; RTI ID = 0.0 &gt; influenza B &lt; / RTI &gt; virus hemagglutinin antigen.

A composition comprising at least three fusion proteins that activate TLR5 may further comprise a fourth fusion protein that activates TLR5. The fourth fusion protein is distinguished from the first influenza B antigen and has an isoelectric point greater than about 8.0, such as from about 8.0 to about 10.0, about 8.5, about 9.0, about 9.5, and about 10.0, and at least one And a second influenza B virus hemagglutinin antigen fused to the loop of the second influenza B virus hemagglutinin antigen.

In certain embodiments, a first fusion protein of a composition comprising at least three fusion proteins each activating TLR5 is conjugated to a &lt; RTI ID = 0.0 &gt; beta- Is a fusion protein comprising two similar portions of influenza A hemagglutinin having a portion of a spherical head with a sheet. The first fusion protein has one HA moiety fused to a portion of the flagellin and another similar HA moiety fused to the carboxy-terminus of a portion of the flagellin in the region where domain 3 is located. An exemplary first fusion protein is SEQ ID NO: 268, which is part of the influenza A California / 07/2009.

In a particular embodiment, a second fusion protein of a composition comprising at least three fusion proteins each activating TLR5 is distinguished from a first influenza A antigen and comprises a second influenza A antigen comprising a second influenza A antigen having an isoelectric point greater than about 7.0 It is a protein. The second influenza A antigen is a β-sheet at the bottom of a portion of the bulbous head of an influenza virus hemagglutinin (referred to herein as "HA1-1L") fused to the R3 construct of a portion of the flagellin, Sandwich and two ß-strands of HA. The HA1-1L antigen replaces domain 3 of the prazoline in the R3 construct. An exemplary second fusion protein is SEQ ID NO: 269, which is part of the influenza A Perth / 16/2009.

In certain embodiments, the third fusion protein of the composition comprising at least three fusion proteins each activating TLR5 has an isoelectric point of greater than about 8.0 and comprises a loop of domain 3 of the third messenger segment, such as SEQ ID NO: 2 Is a fusion protein comprising a first influenza B antigen fused to loop 6 between amino acid residues 277 and 278. An exemplary third fusion protein is SEQ ID NO: 126 (HL772), which is part of influenza B Wisconsin / 1/2010.

In a particular embodiment, the fourth fusion protein of the composition comprising at least three fusion proteins each activating TLR5 has a loop of domain 3 of a portion of the fourth fragment, e. G., SEQ ID NO: 2 Is a fusion protein comprising a second influenza B antigen fused to loop 6 between amino acid residues 277 and 278 of SEQ ID NO: The second influenza B antigen is distinguished from the first influenza B antigen. An exemplary fourth fusion protein is SEQ ID NO: 158 (HL787), which is part of influenza B Bangladesh / 5495/2009.

A "distinct" as used herein in connection with an antigen, protein or prazoline is a first or additional (second, third, fourth etc.) antigen, a first or additional (second, third, Fourth, etc.) protein or a first or additional (second, third, fourth, etc.) pregelatin. For example, the influenza A Perth / 16/2009 hemagglutinin (HA) antigen is distinct from the influenza A California / 07/2009 HA antigen. Similarly, influenza B Wisconsin / 1/2010 HA antigens are distinguished from influenza B Bangladesh / 5495/2009 HA antigens.

Figure 31 shows in turn a fusion protein comprising the amino-domain 0, amino-domain 1, amino-domain 2, carboxy-domain 2, carboxy-domain 1 and carboxy- : 283) of domains D0, D1, D2, D3. The antigen (Ag) is fused between the amino- and carboxy-domain 2 of the prazoline construct. 31 lacks the D3 domain of prazoline and is referred to as " R3 construct "or" R3 form of prazoline "or" R3 prazoline construct "(SEQ ID NO: 283 ). &Lt; / RTI &gt; As used herein, "R3 ( R eplace Domain 3 ) construct" means that domain 3 of the prazoline has been replaced with an antigen as previously described in U.S. Patent Application No. 12 / 905,584. For example, the antigen may be fused between amino acids 190 and 191 of SEQ ID NO: 283.

Figure 32 shows a fusion protein and a fragment construct (SEQ ID NO &lt; RTI ID = 0.0 &gt; NO: &lt; / RTI & : D0, D2, D3) of the cells D0, D2, D4, and D4. For example, the fusion protein depicted in SEQ ID NO: 284 has at least a portion of at least one antigen fused at two sites and at least a portion of at least one other antigen in a portion of the fraxelin. One antigen (also referred to as "first antigen") is fused between amino-domain 2 and carboxy-domain 2 of the prazoline construct. Other antigens that can be distinguished from the first antigen are fused to the carboxy-terminal amino acid of domain 0 of the prazoline construct. 32 lacks the D3 domain of prazoline and is referred to herein as the "R3-2xAg construct" or "R3-2xAg form of prazoline" or "R32x prazoline construct" or "R32x Or "2xR3 form of prazoline" or "R3 / 2x form of prazoline." As used herein, the "R3-2xAg construct" Domain 3 is replaced by one antigen and another antigen, such as a distinct antigen, to be fused to the carboxy-terminus of domain 0 as previously described in U.S. Patent Application No. 12 / 905,584. For example, one May be fused between amino acids 190 and 191 of SEQ ID NO: 284, and another antigen may be fused to the amino acid carboxy terminus (e.g., SEQ ID NOs: 268, 287 and 288).

In yet another embodiment, the first influenza A virus hemagglutinin antigen of the composition of the invention and for use in the methods of the present invention comprises a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head At least a portion of the HA1 subunit having at least a portion; The second influenza A virus hemagglutinin antigen of the composition of the present invention and for use in the method of the present invention comprises at least one [beta] -sheet, at least one [beta] -sandwich and at least two [beta] - all or at least a portion of the HA1 subunit having at least a portion of a spherical head comprising a strand; The first influenza B virus hemagglutinin antigen for use in the method of the invention and of the composition of the present invention comprises an HA1 subunit having at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head All or at least a portion thereof. The second influenza B virus hemagglutinin antigen for use in the method of the present invention and of the composition of the present invention comprises an entire HA1 subunit having at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head Or at least a portion thereof.

In a further embodiment, the first influenza A virus hemagglutinin antigen of the composition of the invention and for use in the method of the invention comprises at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head At least a portion of the HA1 subunit having &lt; RTI ID = 0.0 &gt; The second influenza A virus hemagglutinin antigen of the composition of the present invention and for use in the method of the present invention comprises at least one [beta] -sheet, at least one [beta] -sandwich and at least two [beta] - at least a portion of the HA1 subunit having at least a portion of a spherical head comprising a strand; The first influenza B virus hemagglutinin antigen for use in the method of the invention and of the composition of the present invention comprises an HA1 subunit having at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head At least some of them. The second influenza B virus hemagglutinin antigen for use in the method of the invention and of the composition of the present invention comprises an HA1 subunit having at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head At least some of them.

 In another embodiment, the invention is a method of stimulating an immune response against an antigen in a subject. The method comprising administering to the subject a composition comprising a fusion protein that activates the toll-like receptor 5, wherein the fusion protein binds to at least one loop of domain 3 of Prazoline, And at least one antigen having an isoelectric point of more than &lt; RTI ID = 0.0 &gt; In certain embodiments, an immune response that is stimulated in a subject responsive to administration of a fusion protein provides protective immunity against the disease or infection due to exposure of an organism comprising an antigen fused to the loop of domain 3 of the flagellin. The method may further comprise the administration of an adjuvant.

In yet another embodiment, the invention provides a method of stimulating an immune response in a subject comprising administering to the subject a composition comprising at least three fusion proteins each activating the toll-like receptor 5, wherein (a ) The first fusion protein comprises a first prazoline, and a first influenza A virus hemagglutinin antigen fused to a portion of the first prazoline and having an isoelectric point greater than about 6.0; (b) the second fusion protein comprises a second influenza A virus hemagglutinin fused to a portion of the second plasmin, and having an isoelectric point greater than about 7.0 and distinguished from the first influenza A virus hemagglutinin antigen, Lutinin antigens; (c) the third fusion protein comprises a first influenza B virus hemagglutinin antigen that is fused to at least one loop of domain 3 of the third plasin, and of the third fragment, and has an isoelectric point of greater than about 8.0. Method.

In a further embodiment, the present invention provides a method of stimulating an immune response in a subject, comprising administering to the subject a composition comprising at least four fusion proteins each activating the toll-like receptor 5, comprising: (a) 1 fusion protein comprises a first prazoline, and a first influenza A virus hemagglutinin antigen fused to a portion of the first prazoline and having an isoelectric point greater than about 6.0; (b) the second fusion protein comprises a second influenza A virus hemagglutinin fused to a portion of the second plasmin, and having an isoelectric point greater than about 7.0 and distinguished from the first influenza A virus hemagglutinin antigen, Lutinin antigens; (c) the third fusion protein comprises a first influenza B virus hemagglutinin antigen fused to at least one loop of domain 3 of the third plasine, and a third plasine and having an isoelectric point greater than about 8.0; (d) a fourth fusion protein that activates toll-like receptor 5 is fused to at least one loop of domain 3 of the fourth plasine and has an isoelectric point of greater than about 8.0 and is distinguishable from the first influenza B virus hemagglutinin antigen Lt; RTI ID = 0.0 &gt; influenza B &lt; / RTI &gt; virus hemagglutinin antigen.

In an embodiment, the methods of the invention stimulate the immune response by administering four different fusion proteins (two fusion proteins comprising influenza A antigen and two fusion proteins comprising influenza B antigen), each activating TLR5 signaling do. Four fusion proteins can be administered at increasing doses. For example, initial immunization can be performed with all four fusions (e. G., About 1 pg or about 2 pg), followed by a second dose (e.g., about 2 pg or about 4 pg) Lt; / RTI &gt; protein. Subsequent doses (third or fourth dose) may be used to maintain the dose of the fusion protein comprising influenza A at a dose of about 6 μg to about 8 μg, while maintaining the capacity of the fusion protein comprising about 2 μg or 4 μg of influenza B To &lt; / RTI &gt;

The dose of the fusion protein comprising the influenza A antigen in the multivalent composition ranges from about 2 μg, about 4 μg, about 6 μg, about 10 μg, about 12 μg, about 14 μg, about 15 μg, and about 20 μg And may be at least one member selected. The dose of the fusion protein comprising the influenza B antigen in the multivalent composition may be at least one member selected from the group consisting of about 1 [mu] g, about 2 [mu] g, about 4 [mu] g, about 6 [mu] g, about 8 [mu] g and about 10 [ . The multicomponent composition comprises a composition of the present invention having at least three fusion proteins, for example, a composition comprising two fusion proteins with an influenza A antigen and one or two fusion proteins with an influenza B antigen. The fusion protein of the composition to be administered to the subject may comprise about 1 μg, about 2 μg, about 3 μg, about 4 μg, about 5 μg, about 6 μg, about 7 μg, about 8 μg, about 9 μg, about 10 μg, A dose of at least one member selected from the group consisting of 15 μg dose, about 20 μg dose, about 25 μg dose, about 30 μg dose, about 35 μg dose, about 40 μg dose, about 45 μg dose and about 50 μg dose .

In yet another embodiment, the invention is a method of stimulating an immune response against influenza A and influenza B antigens in a subject. The method comprises administering to a subject a composition comprising SEQ ID NOs: 268, 269, 126, and 158.

The method of the present invention may further comprise administering an adjuvant.

As used herein, an " immune response stimulus "refers to an antigen fused to the loop of domain 3 of flazelin, such as the protein portion of influenza B hemagglutinin (HA) described herein (e.g. HA1-1, RTI ID = 0.0 &gt; HA1-2, &lt; / RTI &gt; HA1-1L protein). Immunoreactive stimulation in a subject can include the generation of humoral and / or cellular immune responses that are reactive against an antigen, such as a viral protein, particularly influenza virus protein.

Compositions of the invention for use in the present methods for stimulating an immune response in a subject can be evaluated for their ability to stimulate an immune response in a subject using well established methods. Exemplary methods for determining whether a composition of the invention stimulates an immune response in a subject include, but are not limited to, the generation of antibodies (e.g., IgG antibodies) specific for an antigen by ELISA assays; The possibility of inducing antibody-dependent enhancement (ADE) of secondary infection; Macrophage-like assay; Neutralization evaluated using the Plaque Reduction Neutralization Test (PRNT ₈₀ ); (Putnam, et al., Vaccine 23: 4442-4452 (2005)) in an animal model (e. G., Mouse, rabbit, monkey).

As used herein, the term "stimulate a protective immune response" refers to administration of a composition of the invention comprising a fusion protein comprising, for example, an influenza B antigen fused to at least one loop of domain 3 of the flagellin Which induces the production of antibodies to the protein, which causes the subject to tolerate an attack by a viral protein, for example, an influenza B virus attack, which would otherwise have been lethal. Techniques for measuring lethal viruses (e. G. Influenza B viruses) are known to those skilled in the art (see, for example, WHO / CDS / CSR / NCS2002.5 &quot; WHO Manual on Animal Influenza Diagnosis and Surveillance & Harmon, MW, et al., J. Clin. Microbiol. 26: 333-337 (1988); Reed, LJ, et al., Am. 23: 937-943 (1999); Walls, HH et al., J. Clin. Microbiol., 23: 493-497 (1938); Rose, T., et al., J. Clin. Microbiol. Cottes, R., et al., John Wiley &amp; Sons, Inc (2001)). An exemplary technique for measuring lethal dose is to administer viral doses of varying doses of virus and doses (e.g., LD ₁₀ , LD ₂₀ , LD ₄₀ , LD ₅₀ , LD ₆₀ , LD ₇₀ , LD ₈₀ , LD ₉₀ ) And may include a percentage measurement of a living subject. For example, the lethal dose of virus resulting in 50% mortality of the population of subjects is referred to as "LD ₅₀ &quot;; The lethal dose of virus resulting in 80% mortality of the population of subjects is referred to herein as "LD ₈₀ &quot;; The lethal dose of virus resulting in 90% mortality of the population of subjects is referred to herein as "LD ₉₀ &quot;.

For example, measurement of LD ₉₀ can be carried out intranasally at various doses (e. G., A log and half-log dilution of a diluent, e. G. 8 x 10 ³ egg-infectious dose (EID) (E. G., A mouse) by assessing the survival of the subject at &lt; / RTI &gt; 14 days to about 21 days. Protective immunity can be assessed by physical appearance, general behavior (activity), body weight (initial weight loss, return to body weight close to the body weight of the subject prior to viral infection) and survival after about 14 to about 21 days after infection with the virus &Lt; / RTI &gt;

Assessment of the stimulation of protective immunity may also be used to detect viral proteins (e. G., Viral proteins, e. G., Influenza B virus antigens, e. G., Portions of hemagglutinin) (See, for example, Current Protocols in Immunology, 19.11.1-19.11.32, Cottey, R., et al., J. Immunol. et al., John Wiley & Sons, Inc (2001)). Assessment of stimulation of protective immunity can also be accomplished by using assays that measure the ability of the antibody to inhibit hemagglutinin binding (see, for example, Burnett, FM, et al., J. exp. Biol. Med. Sci. 25: 227-233 (1947); Salk, JEJ Immunol. 49: 87-98 (1944); Current Protocols in Immunology, 19.11.1-19.11.32, Cottey, R., et al., John Wiley & Sons, Inc (2001)).

Inhibition of hemagglutinin binding is an indicator of the ability of the antibodies formed from the compositions of the invention and by the methods of the invention to neutralize ("HA binding neutralization") the sialic acid binding site of the naturally occurring virus hemagglutinin , Whereby infection of the host cell is prevented as a result of stimulation of the protective immune response. Inhibition or neutralization of hemagglutinin binding is believed to be related to the ability of the immune response to protect against lethal viruses.

Neutralization of HA binding can be assessed by in vitro assays (see, for example, Current Protocols in Immunology 19.11.1-19.11.32, Cottey, R., et al., Suppl. 42, John Wiley & Sons , Inc. (2001) and WHO Manual on Animal Influenza Diagnosis and Surveillance, Webster, R., et al., Pages 28-36, 48-54, 82-92 (2002)). Exemplary viral neutralization assays are dependent on the ability of the serum to specifically bind to influenza virus and prevent its replication in cultures such as the Madin-Darby Canine Kidney (MDCK) cell line. Briefly, cells are cultured in 96 well plates in the presence of pre-titered virus and the cytopathic effects of the replication virus are observed under a microscope. To evaluate the sera, serial dilutions of serum are prepared and preincubated with the virus stock at 37 ° C for about 2 hours before infection with MDCK cells. The virus / serum mixture is removed and replaced with fresh medium and the mixture is incubated for an additional 2 hours. Cells are grown for 4 days. Wells were recorded as positive for viral growth when at least about 50% of the cells were killed in at least about half of the wells for the serum dilutions. The inverse of the highest dilution of serum that protects at least about half of the cells from lethality in at least about half of the wells is considered neutralization.

Alternatively, micro-neutralization in vitro assays can be performed to assess neutralization of HA binding. For example, as described above, serum is diluted and preincubated with virus of known activity and mixed with MDCK cells. After 2 days of incubation, cells are washed and fixed with acetone. Plates were developed with ELISA using monoclonal antibodies against influenza nuclear antigen NP. The micronutrient level is measured as the inverse of the highest dilution that leads to less than about 50% of the anti-NP assay of control wells containing only the virus.

The HAI assay is based on HA antigens on the surface of influenza viruses that interfere with red blood cells (RBCs) and prevent red blood cells from settling. Antibodies that specifically bind to the sialic acid-binding region of HA prevent stiction and allow precipitation. The assay is performed in a 96 well V bottom plate using fresh chicken RBC. The stock of the viral antigen is titrated such that approximately four-fold excess of antigen is present for the minimum amount necessary to prevent precipitation. Test sera, which may result from several species, including mice, ferrets, poultry or humans, are heated to about 56 ° C to completely inactivate them. A two-fold serial dilution of inactivated serum is performed and mixed with stock HA. After about 30 minutes at room temperature, RBC is added and the plate is incubated for about 30 to about 45 minutes. Observe results: The stiction induces turbid wells while the inhibition induces the "button" of erythrocytes precipitated in the well bottom. Controls include HA-free RBCs that form buttons and serum-free HA and RBCs that remain cloudy. The HAI reversal of a particular serum sample is the reciprocal of the last dilution to prevent clogging (i.e., button formation). For example, if the 1: 128 dilution is interpreted as a button and the 1: 256 dilution is not, the HAI reversal is about 128.

Fusion proteins of the invention can be prepared using routine molecular biology techniques as described herein. The host cell may be transfected with a nucleic acid encoding a fusion protein of the invention. Host cells can be eukaryotic or prokaryotic host cells. Suitable prokaryotic host cells include E. coli, B. subtilis (B. subtilis) and Pseudomonas fluorescein sense (Pseudomonas fluorescens .

The eukaryotic host cells used in the methods of the present invention include, but are not limited to, Saccharomyces eukaryotic host cells, insect eukaryotic host cells (e. G., Baculovirus-infected insect cells such as Spodoptera frugiperda (Sf9) or Trichhoplusia ni (High5) cells; And at least one member selected from the group consisting of Drosophila insect cells such as Dme 12 cells), fungal eukaryotic host cells, parasitic eukaryotic host cells (e. G., Leishmania tarentolae eukaryotic host cells ), CHO cells, yeast cells (e.g., Pichia), and Kluyveromyces lactis lactis ) host cells.

Suitable eukaryotic host cells and vectors may also be derived from plant cells (e. G., Tomatoes; chloroplasts; monocotyledonous and dicotyledonous plant cells; Arabidopsis thaliana ; Hordeum vulgare ); Zea mays ; Potatoes, for example, Solanum tuberosum ); Carrots such as Daucus carota L .; And tobacco, such as Nicotiana &lt; RTI ID = 0.0 &gt; tabacum , Nicotiana &lt; RTI ID = 0.0 &gt; Benthamiana ) (Gils, M. et al., Plant Biotechnol J. 3: 613-20 (2005); He, DM, et al., Colloids Surf B Biointerfaces, , Marquet-Blouin, E., et al., Plant Mol Biol (2003), Vaccine 19: 2163-71 (2001); Khandelwal, A., et al., Virology 308: Varsani, A., et al., Virus Res, 120: 91-6 (2006); Plant Biotechnol J. 4: 551-9 (2006); Infect Immun. 73: 8266-74 (2005); Zhang, X., et al., Plant Biotechnol. J. 4: 419-32 (2006)).

The fusion proteins of the present invention can be purified and characterized using well known methods (e.g., gel chromatography, cation exchange chromatography, SDS-PAGE) as described herein.

For large scale production, fermentation techniques can be used. An exemplary fermentation technique may include a proposed cycle that is inoculated with 6 L of MRBR medium as described herein, and can be started at about 30 DEG C, maintained at about pH 7, and about DO controlled at about 30% . Subsequently, 6 liters of feed can be started at least about 30 minutes after glucose depletion. When combined with 6 L of MRBR medium, the proposed 6-liter feed medium can provide a requirement for E. coli growth based on approximately 52% carbon utilization for growth. The feed may or may not include IPTG. At least 2 mM IPTG introduced as a bolus may be introduced into the batch immediately after the commencement of production and commencement of production. The feed rate can be started with a volume of about 20 mL feed / hour / liter bioreactor and is increased over time based on the ability of the culture to allow more glucose without glucose accumulation. When the supply is complete, the culture may be harvested. The 6 liter feed medium (approximately pH 6.0) contained glucose 180 g / L; KH ₂ PO ₄ 2 g / L; _{NaH 2 PO 4 (H 2 O} ) 4 g / L; _{(NH 4) 2 HPO 4 12} g / L; _{(NH 4) 2 HSO 4 4} g / L; DL-alanine 40 g / L; 4 g / L citric acid; _{MgSO 4 (7H 2 0) 5.5} g / L; Trace metal 6 mL; CaCl ₂ 2.5 g / L; FeSO ₄ 7H ₂ O 1 g / L.

Cell destruction and purification in large scale production include removal of Triton X-100 from resuspension buffer; Dissolution of insolubles by addition to 50 mM Tris, 25 mM NaCl, 8 M urea, cell lysate at about pH 8; Nucleic acid removal and / or assisted filtration by addition of PEI (polyethylamine) and subsequent removal by centrifugation with one or more buffers; The addition of flocculants such as AEROSIL 380, AEROSIL 200, ALKOXIDE ALU C, and CELPUR; And subsequent removal by centrifugation for auxiliary filtration. Cation exchange chromatography can include the use of process resins, urea up to 8 M and addition of a denaturing endotoxin removal step containing up to about 2% Triton X-100 and step gradient elution. The step elution gradient may comprise about 100 to about 200 mM NaCl.

In a further embodiment, the invention provides a pharmaceutical composition comprising at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95% 98% and at least about 99% sequence identity.

The percent identity of two amino acid sequences (or both nucleic acid sequences) can be determined by sequence alignment for optimal comparison purposes (e. G., The gap can be introduced into the sequence of the first sequence). Then, the amino acid sequence or nucleic acid sequence at the corresponding position is compared, and the percent identity between the two sequences is a function of the number of identical positions shared by the sequence (i.e.,% identity = total # x 100 ). Protein or nucleic acid encoding lengths that can be aligned for comparison purposes include the R3 sequences used in the fusion sequences of the invention (e. G., SEQ ID NOs: 126, 158, 268 and 269) (E.g., SEQ ID NO: 283) or R32x construct (e.g., SEQ ID NO: 284, 285), prazoline (SEQ ID NO: At least about 75%, at least about 80%, at least about 85%, at least about 85%, at least about 85%, at least about 85%, at least about 85% , At least about 95%, at least about 98%, at least about 99%.

Substantial comparison of two sequences can be accomplished, for example, by well-known methods using mathematical algorithms. A preferred non-limiting example of such a mathematical algorithm is described in Karlin et al. (Proc. Natl. Acad. Sci. USA, 90: 5873-5877 (1993), the teachings of which are incorporated herein by reference in their entirety.) Such algorithms are described, for example, in Schaffer et into the BLASTN and BLASTX programs as described in Nucleic Acids Res., 29: 2994-3005 (2001) and Oehmen, CS et al., Bioinformatics 29 (6): 797-798 (2013). When using BLAST and Gapped BLAST programs, default parameters of each program (e.g., BLASTN: available from the Internet site of the National Center for Biotechnology Information) may be used. , The examined database is a non-overlapping (NR) database and the parameters for the sequence comparison can be set as follows: unfiltered; predicted value 10; word size 3; matrix is BLOSUM62; gap cost Cost) is the value of this Having an extension (Extension) 1.

Another mathematical algorithm used for sequence comparison is Myers & Miller's algorithm CABIOS (1989). These algorithms are integrated into the ALIGN program (version 2.0), which is part of the GCG (Accelrys, San Diego, California) sequence alignment software package. When using the ALIGN program for amino acid sequence comparison, a PAM120 weight residue table, a gap length penalty of 12 and a gap penalty of 4 are used. Additional algorithms for sequencing are known in the art and described in Torellis, et al., Comput. Appl. ADVANCE and ADAM as described in Biosci., 10: 3-5 (1994) and FASTA as described in Pearson, et al., (Proc. Natl. Acad. Sci USA, 85: 2444-2448 , The teachings of which are incorporated herein by reference in their entirety.

The% identity between two amino acid sequences can also be calculated using the GAP program in the GCG software package using a Blossom 63 matrix or a PAM250 matrix, gap weights 12, 10, 8, 6, or 4, and length weights 2, 3, (Accelrys, San Diego, Calif.). In yet another embodiment, percent identity between two nucleic acids can be achieved using the GAP program (Accelrys, San Diego, Calif.) In a GCG software package with gap weight 50 and length weight 3.

The nucleic acid sequence encoding the protein portion of the HA, polypeptide, or fusion protein of the present invention and the polypeptide of the present invention may comprise a nucleic acid sequence of the invention, for example, an antigen, an R3 construct or an R32x construct used in the fusion protein of the invention (E.g., hybridization conditions of high stringency) to a complementary sequence of the nucleic acid sequence or nucleic acid sequence of the contained promoter. The nucleic acid sequence may be hybridized under selective hybridization conditions (e. G., High stringency hybridization conditions). The term "low stringency hybridization", "medium stringency hybridization", "high stringency hybridization" or "very high stringency hybridization" as used herein describes hybridization and nucleic acid sequence washing conditions . Guidance for performing hybridization reactions that may include aqueous and non-aqueous methods can be found in Aubusel, FM, et al., Current Protocols in Molecular Biology, John Wiley & Sons, N.Y. (2001).

For applications requiring high selectivity, relatively high stringency conditions may be used to form the hybrid. In solutions used in some membrane-based hybridization, the addition of an organic solvent such as formamide allows the reaction to occur at low temperatures. High stringency conditions are, for example, relatively low salt and / or high temperature conditions. High stringency conditions are provided by about 0.02 M to about 0.10 M NaCl at a temperature of about 50 &lt; 0 &gt; C to about 70 &lt; 0 &gt; C. The condition of high stringency allows for a limited number of mismatches between the two sequences. To achieve less stringent conditions, the salt concentration can be increased and / or the temperature can be reduced. Medium stringency conditions are achieved at a salt concentration of about 0.1 to 0.25 M NaCl and a temperature of about 37 ° C to about 55 ° C while a low stringency condition is achieved at a salt concentration of about 0.15 M to about 0.9 M NaCl, RTI ID = 0.0 &gt; 55 C. &lt; / RTI &gt; Component selection and hybridization conditions are well known to those skilled in the art and are described in Ausubel et al., Short Protocols in Molecular Biology, John Wiley &amp; Sons, New York NY, Units 2.8-2.11, 3.18-3.19 and 4-64.9, 1997).

As used herein, a "subject" can be a mammal, such as a primate or rodent (eg, a mouse, a mouse). In certain embodiments, the subject is a human.

&Quot; Effective amount "when referring to an amount of the composition and fusion protein of the present invention refers to the amount of fusion protein and composition that, when administered to a subject, is sufficient for therapeutic efficacy (e.g., an amount sufficient to stimulate an immune response in the subject) Or capacity. The compositions and fusion proteins of the invention may be administered in single or multiple doses.

The method of the present invention can be accomplished by administering the fusion proteins and compositions of the present invention by intestinal or parenteral means. Specifically, the route of administration is by oral ingestion of the composition and fusion protein (e. G., Drink, tablet, capsule) or intramuscular injection. Intravenous, intradermal, intraarterial, intraperitoneal or subcutaneous routes and other routes of administration, including non-administration, are also encompassed by the present invention. Suppositories or transdermal patches may also be used.

The compositions and fusion proteins of the present invention may be administered ex vivo as autologous dendritic cells of a subject. Following exposure of the dendritic cells to the fusion proteins and compositions of the invention, the dendritic cells may be administered to the subject.

The compositions and fusion proteins of the invention may be administered alone or co-administered to a patient. Co-administration is meant to include simultaneous or sequential administration of the compositions, fusion proteins or polypeptides of the invention, either individually or in combination. When the composition and the fusion protein are administered separately, the mode of administration is performed within a time sufficiently close to each other (e. G., Administration of the composition in close proximity to the administration of the fusion protein) to maximize the stimulatory effect of the immune response in the subject. It is also contemplated that administration of multipath (e.g., intramuscular, oral, transdermal) may be used to administer the compositions and fusion proteins of the present invention.

The compositions and fusion proteins of the present invention may be administered alone or in admixture with conventional excipients such as, for example, pharmacologically or physiologically acceptable organic or inorganic carrier materials, which do not deleteriously react with the extract and are suitable for enteral or parenteral application . Suitable pharmaceutically acceptable carriers include water, salt solutions (e. G., Ringer's solution), alcohols, oils, gelatin and carbohydrates such as lactose, amylose or starch, fatty acid esters, hydroxymethylcellulose and polyvinylpyrrolidine. Such products may be sterilized and, if necessary, supplemented with adjuvants that do not deleteriously react with the compositions, fusion proteins or polypeptides of the present invention such as lubricants, preservatives, stabilizers, wetting agents, emulsifiers, salts for influencing osmotic pressure, Colorants and / or aromatic materials and the like. Such products may also be combined with other active substances to reduce metabolic deterioration, if desired. The compositions and fusion proteins of the present invention may be administered by oral administration, for example, by intramuscular, intramuscular or intraperitoneal injection or intranasal delivery. The compositions and fusion proteins may be administered alone or in combination with a single agent over a period of time to provide a desired effect (e. G., Relief of virus infection such as influenza or flavivirus infection, prevention, Dose or more than once.

When parenteral application is required or desired, a particularly suitable mixture of the composition and the fusion protein is an implantable sterile solution, preferably an oil or aqueous solution and an implant comprising a suspension, emulsion or suppository. In particular, carriers for parenteral administration include aqueous solutions of dextrose, saline, pure water, ethanol, glycerol, propylene glycol, peanut oil, sesame oil, polyoxyethylene-block polymers, and the like. Ampoules are a convenient unit dosage form. The compositions, fusion proteins or polypeptides may also be incorporated into liposomes or administered via a transdermal pump or patch. Pharmaceutical mixtures suitable for use in the present invention are well known to those skilled in the art and are described for example in Pharmaceutical Sciences (17th Ed., Mack Pub. Co., Easton, PA) and WO 96/05309 , The teachings of which are incorporated herein by reference.

The compositions and fusion proteins of the present invention can be administered to a subject on a support to present the compositions, fusion proteins and polypeptides of the invention to the immune system of the subject to generate an immune response in the subject. Presentation of the compositions, fusion proteins, and polypeptides of the invention will preferably include generating an antibody by exposing the antigenic portion of the viral protein. The fusion proteins of the invention are located physically close together on a support. The fusion protein of the present invention can be attached to a support by covalent or noncovalent bonding. Preferably, the support is biocompatible. As used herein, "biocompatibility" means that the support does not produce an immune response (e. G., Antibody production) in the subject. The support may be a biodegradable matrix carrier such as polymer beads or liposomes. The support may further comprise alum or other suitable adjuvant. The support may be a virus (e.g., adenovirus, a poxvirus, an alphavirus), a bacteria (e.g. salmonella) or a nucleic acid (e.g. plasmid DNA, CpG).

The dose and frequency (single or multiple doses) administered to a subject can be determined by prior exposure to the antigen, the viral protein, the duration of the viral infection, the pretreatment of the viral infection, the route of administration of the composition or fusion protein; Age, sex, health status, weight, body mass index and eating habits; (E. G., Influenza virus) or other antigens such as influenza antigen treatment or infection, concurrent treatment types, complications due to virus exposure, viral infection &lt; RTI ID = 0.0 & Or various factors including exposure or other health related problems. Other therapeutic regimens or agents may be employed with the methods and compositions of the invention and fusion proteins. For example, administration of the composition and the fusion protein can be accomplished by the use of an agent for treating symptoms of a disease associated with or resulting from exposure to an antigen, such as an influenza infection, or by other viral therapy. Control and manipulation of established medications (e.g., frequency and duration) are within the ability of those skilled in the art.

Exemplary portions of antigens, prazoline and fusion proteins of the present invention include those listed in Table 1.

Table 1

Additional portions of antigen, prazoline and fusion proteins for use in the present invention may include those listed in Table 2. For example, the fusion protein may comprise a portion of the globular head of HA fused to loop 6 of domain 3 of S. typhimurium FljB plasmid at the D3I-o1 insertion site between residues 276-277 of SEQ ID NO: 127 .

Table 2

adduction

Example 1. Primary Sequence Analysis of Prazoline for Targeting Influenza B by Confirming Antigen Insertion Site

Primary sequence analysis showed that a portion of the influenza virus hemagglutinin, for example the amino acid sequence of HA1-2 of the Flu B (influenza B) spherical head (SEQ ID NOs: 45, 47 and 61) Lt; RTI ID = 0.0 &gt; SEQ ID &lt; / RTI &gt; NO: 63. At neutral pH, a portion of the Influenza Flu B spherulised head, e.g., SEQ ID NO: 45, has a net positive charge and a pI of about 8.5 to about 9.5. At neutral pH, Prazoline partially has a net negative charge due to a series of negatively charged amino acids in domain 1 (D1) of the prazoline with a pI of about 4.5 to about 5.0. Attachment of positively charged portions of influenza B HA and negatively charged D1 of prazoline, such as R3 and R3.2x fusion proteins, can induce intramolecular interactions between a portion of prazoline and a portion of HA, The ability of the flagellin to trigger TLR5 signaling and the presentation of influenza B HA antigen to immune cell receptors.

As in the case of HL098 (SEQ ID NO: 122), the immunogenicity of the R3 fusion protein of a composition comprising influenza B, such as B / Florida / 4/2006, SEQ ID NO: 123). &Lt; / RTI &gt; For example, an additional nine amino acids (SLPLIGEAD (SEQ ID NO: 123) HA1-2 (e.g., SEQ ID NO: 45) of HA corresponding to native amino acid residues 300-308 of SEQ ID NO: May be added to the carboxy-terminus of HA to generate SEQ ID NO: 46. For example, HA1-2 with an extension may then be used to generate a fusion protein, such as HL352 (SEQ ID NO: 125). (E. G., SEQ ID NO: 123) introduced two negatively charged amino acids (E306 and D308) into a portion of the spherical head, Acting as a "pushing away " to move away from charged charged praxelin. However, as described below, the activity associated with a fusion protein having an HA element with an additional 9 amino acids, 3 and 5, and "HL098" (SEQ ID NO: 122) and "HL352" (SEQ ID NO: 125).

Fusion of an antigen with an isoelectric point of greater than about 7.0 to the loop of domain 3 of the praxelin results in the presence of the HA antigenic element of the fusion protein away from the domain (D1) (TLR5-binding domain) of the prazoline &Lt; / RTI &gt; An influenza virus hemagglutinin, such as influenza B virus hemagglutinin, comprising at least a portion of a spherical head having at least one [beta] -sheet at the bottom of the spherical head and having an isoelectric point of greater than about 7.0, SEQ ID NOs: 45, 61) may be fused within at least one loop of domain 3 of the pregulin to form a "D3Ins format" (also referred to as "D3I" or "D3I construct"). Likewise, a portion of influenza virus hemagglutinin, including at least a portion of a spherical head having at least one [beta] -sheet at the bottom of the spherical head, having an isoelectric point greater than about 7.0, such as influenza A virus of SEQ ID NO: 98 Hemagglutinin and A / Perth / 16/2009 strains can be fused into at least one loop of domain 3 of the praxylene to form the "D3Ins format &quot;. A fusion protein comprising both influenza A and influenza B antigens may be combined to target both influenza A and influenza B antigens to form a multivalent composition that prevents or minimizes disease associated with influenza A and influenza B infection.

The crystal structure of domain 3 of Salmonella typhimurium protuberance (FliC, Protein Data Bank ID (PDB): 1UCU) has been reported (Yonekura, K., et al., Nature, 424: 643-650 (2003) ), Identified six loops of domain 3 of SEQ ID NO: 1. The secondary structure prediction of Salmonella typhimurium pyrazoline FliC using PHD is described below and is consistent with the known tertiary structure and predicts six loops in domain 3. The names are: AA: primary amino acid sequence; PROF_sec: secondary structural prediction (Rost, B., et al., Proteins, 19: 55-72 (1994)), where "H" denotes α-helix and "E" denotes β-strand. The predicted loop of domain 3 of SEQ ID NO: 1 was boxed below. The secondary structure adjacent to the predicted loop was essentially similar to the known secondary structure for Salmonella typhimurium prazoline (Protein Data Bank ID (PDB): 1UCU) (Yonekura, K., et al., Nature , 424: 643-650 (2003)).

The predicted secondary structure of FliC (S. typhimurium, SEQ ID NO: 1) was substantially similar to known high-resolution atomic models as measured by a combination of X-ray crystallography and electron microscopy (1UCU, Yonekura, K., et al., Nature, 424: 643-650 (2003)). Substantial similarity between the predicted secondary structure of S. typhimurium FliC (SEQ ID NO: 1) and the known secondary structure is shown in Figure 1 (a), with the exception of S. typhimurium FljB (SEQ ID NO: A secondary structure predicted using CLUSTALW and PHD, adjacent to the loop of domain 3, can be used, for example, to select an insertion site corresponding to a known loop of domain 3 in another plasin of S. typhimurium FliC .

Secondary structure prediction using PHG of Prazoline FliC (Salmonella typhimurium, Protein Data Bank ID: 1UCU, SEQ ID NO: 1) is described below. The predicted loop in domain 3 was boxed.

Secondary structure prediction using PHJ of pravagelin FljB (S. typhimurium, SEQ ID NO: 2). The predicted loop of domain 3 is represented by the text in the box.

Prediction of the loop of domain 3 using PHD compared to known loops identified by X-ray crystal analysis can be used to predict the amino acid sequence and loop for the insertion site of the antigen in domain 3 of the phagelin of the PHD computer program .

The sequence alignment between S. typhimurium FliC (SEQ ID NO: 1) and S. typhimurium FljB (SEQ ID NO: 2) is PROF_sec: structure prediction where "H" represents alpha- "Beta-was performed using a secondary structure prediction and multiple sequence alignment tool according to the PHD using the CLUSTALW shows a strand) (.. Thompson, JD, et al, Nucleic Acids Res 22: 4673-4680 (1994); Rost , B., et al., Proteins 19: 55-72 (1994)). The following sequence listing showed about 74.75% identity of the amino acid residues denoted by (*), a strongly similar (about 7.30%) homologous amino acid residue of about 7.69% and a difference of about 10.26% Respectively. The domain boundaries of D0 , D1 , D2, and D3 are underlaid differently and three D3 insertion sites are indicated.

The purpose of this sorting is to identify the known loops of domain 3 of S. typhimurium FliC (SEQ ID NO: 1) for the insertion point of the portion of HA with an isoelectric point of greater than about 7.0 to produce the fusion protein of the present invention Region of domain 3 of S. typhimurium FljB (SEQ ID NO: 2) corresponding to the region of interest.

The primary difference between Salmonella typhimurium FliC (PDB: 1UCU (Yonekura, K., et al., Nature , 424: 643-650 (2003), SEQ ID NO: 1) and FljB (SEQ ID NO: 2) The amino acid sequence alignment showed that the two plasins share the highly conserved D0 (domain 0) and D1 (domain 1) domains but change in the D2 (domain 2) and D3 (domain 3) domains. However, the secondary structure prediction using PHD (Rost, B., et al., Proteins 19: 55-72 (1994)) is based on the FliC prazoline FliC (SEQ ID NO: 1) and FljB praxelin of Salmonella typhimurium (SEQ ID NO: 2) share a similar secondary structure, despite differences in the primary amino acid sequence.

Sequence alignment and secondary structure prediction using the PHI and CLUSTALW of FliC (SEQ ID NO: 1) and FljB (SEQ ID NO: 2) of S. typhimurium are shown below. The predicted loop of domain 3 is represented by the text in the box.

The insertion site in the predicted loop of domain 3 of S. typhimurium FljB is referred to herein as "D3I-o1 ", and the amino acid residue of SEQ ID NO: 2 for fusion of the antigen with an isoelectric point greater than about 7.0 G277 and A278. The insertion site D3I-o1 is between the predicted? -Structure VTLA (SEQ ID NO: 131), which is the amino acid residue 263-266 of SEQ ID NO: 2, and the VVS, which is the amino acid residue 293-295 of SEQ ID NO: 2. Another insertion site in the second predicted loop of domain 3 of S. typhimurium FljB is referred to herein as "D3I-i1 " and is present between residues T259 and D260 of SEQ ID NO: 2. The insertion site D3I-i1 comprises a beta -start EVNVA (SEQ ID NO: 132) corresponding to amino acid residues 254-258 of SEQ ID NO: 2 and a VTLA (SEQ ID NO: 132) corresponding to amino acid residues 263-266 of SEQ ID NO: NO: 131). The additional insertion site in the third predicted loop of domain 3 of S. typhimurium FljB is referred to as "D3I-s1" and is between residues G244 and A245 of SEQ ID NO: 2. The insertion site of D3I-s1 is the? -Strip KYFVTIGG (SEQ ID NO: 133) corresponding to amino acid residues 234-241 of SEQ ID NO: 2 and the EVNVA (SEQ ID NO: 133) corresponding to amino acid residues 254-258 of SEQ ID NO: ID NO: 132). The secondary structure adjacent to the predicted loop of S. Typhimurium FliC is substantially similar to the predicted secondary structure adjacent to the loop of domain 3 of S. typhimurium FljB, as shown in FIG.

In embodiments, the fusion of the antigen with an isoelectric point greater than about 7.0 can be from about 2 to about 10 amino acids from the designated insertion site toward the carboxy- or amino-terminus of the prazoline, based on the proximity of adjacent secondary structural elements have. For example, the D3I-o1 site may be the amino acid residues G268 to D289 of SEQ ID NO: 2 which do not invade the adjacent [beta] -string and the VTLA (SEQ ID NO: 2) at amino acid residues 263-266 of SEQ ID NO: : 131) and the VVS at amino acid residues 293-295 of SEQ ID NO: 2. Also, for example, the D3I-i1 region comprises an EVNVA (SEQ ID NO: 132) at amino acid residues 254-258 of SEQ ID NO: 2 and a VTLA (SEQ ID NO: 132) at amino acid residues 263-266 of SEQ ID NO: Amino acid residues D260 of SEQ ID NO: 2 or only one or two amino acid shifts toward the carboxy-terminal end of the pregulin of SEQ ID NO: 2 in G261 Can be accommodated.

Based on the predicted secondary structure analysis, a loop of domain 3 of E. coli FliC prazoline (SEQ ID NO: 3) and Pseudomonas aeruginosa PAO1 prazoline (SEQ ID NO: 4) can be predicted. Based on this analysis, the E. coli FliC primary amino acid sequence (SEQ ID NO: 3) was aligned with the primary amino acid sequence of Salmonella typhimurium FliC (SEQ ID NO: 1). The secondary structure is Salmonella typhimurium FliC. (SEQ ID NO: 1), or by prediction using the PHD. The secondary structure of E. coli praxelin (SEQ ID NO: 3) or Pseudomonas aeruginosa PAO1 prazoline (SEQ ID NO: 4) was designated using the PHD program. The designation is depicted as AA: primary amino acid sequence; PROF_sec: secondary structure prediction, where "H" represents α-helix and "E" represents the β-strand (Rost, B., et al., Proteins 19: 55-72 (1994)).

Secondary structure prediction using PHG of Frajelin FliC (E. coli, SEQ ID NO: 3) is described as follows. The predicted loop of domain 3 is represented by the text in the box.

The secondary structure prediction using PHG of prazoline (P. aeruginosa PAO1 , SEQ ID NO: 4) is depicted as follows. The predicted loop of domain 3 is represented by the text in the box.

The E. coli FliC primary amino acid sequence (SEQ ID NO: 3) was initially aligned with the primary amino acid sequence of Salmonella typhimurium FliC (SEQ ID NO: 1). Sequence alignment uses a secondary structure prediction by PHD using multiple sequence alignment tools CLUSTALW and PROF_sec: (representing a secondary structure prediction, where "H" represents alpha-helix and "E" represents the beta-strand) (Thompson, JD, et al., Nucleic Acids Res . 22: 4673-4680 (1994); Rost, B., et al., Proteins 19: 55-72 (1994)). The sequence alignment showed about 53.98% identity of the amino acid residues denoted by (*), a strongly similarity of about 12.95%, a weakly similar amino acid residue of about 11.16% (~) and a difference of about 21.91% . The predicted secondary structure of E. coli FliC (ECFlic, SEQ ID NO: 3), despite the differences in the primary amino acid sequence, is similar to that of STFliC, Protein Data Bank ID: 1UCU (Yonekura, K., et al., Nature 424: 643-650 (2003)).

Sequence alignment with PHD and CLUSTALW of S. typhimurium FliC (SEQ ID NO: 1) and E. coli FliC (SEQ ID NO: 3) to select the loop of domain 3 for fusion to the antigen Structural predictions are described below. The predicted loop of domain 3 is represented by the text in the box.

Sequence alignments of Salmonella typhimurium FliC (STFlc, Protein Data Bank ID: 1UCU, SEQ ID NO: 1) and Pseudomonas aeruginosa PAO1 praxelin (SaFlix1, SEQ ID NO: 4) were performed using the multiple sequence alignment tools CLUSTALW and PROF_sec (Thompson, JD, et al., (1996)), which is based on the prediction of secondary structure by PHD using the following formula: (represents secondary structural prediction, where "H" represents alpha-helix and "E" represents beta- Nucleic Acids Res . 22: 4673-4680 (1994); Rost, B., et al., Proteins 19: 55-72 (1994)). The sequence alignment showed about 36.24% identity of the amino acid residues denoted by (*), a strong similarity of about 20.59%, a weakly similar amino acid residue of about 13.07%, and a difference of about 30.10% .

CLUSTALW and S. typhimurium FliC (SEQ ID NO: 1) and P. aeruginosa PAO1 pregulin (SEQ ID NO: 4) were used to select the loop in domain 3 of the pregulin for fusion to the antigen Sequence alignment and secondary structure prediction using the PHD of FIG. The predicted loop of domain 3 is represented by the text in the box.

The insertion site in the loop of domain 3 of S. typhimurium FljB (SEQ ID NO: 2) for fusion to an antigen whose isoelectric point is greater than about 7.5, referred to herein as "D3I-o1 & Stranded VTLA (SEQ ID NO: 131), which is the amino acid residue 263-266 of SEQ ID NO: 2, and VVS, which is the amino acid residue 293-295 of SEQ ID NO: 2. The insertion site in the loop of domain 3, referred to herein as "D3I-i1 ", comprises the beta -chain EVNVA (SEQ ID NO: 132) and VTLA (SEQ ID NO: 132) corresponding to amino acid residues 254-258 of SEQ ID NO: SEQ ID NO: 131, corresponding to amino acid residues 263-266 of SEQ ID NO: 2). The insertion site in the loop of domain 3, referred to herein as "D3I-s1 ", comprises the beta -chain KYFVTIGG (SEQ ID NO: 133) and FljB (S. tie) corresponding to amino acid residues 234-241 of SEQ ID NO: (SEQ ID NO: 132) corresponding to the amino acid residues 254-258 of SEQ ID NO: 2 in SEQ ID NO: 2). The D3I-o1, D3I-i1 and D3I-s1 insertion sites predicted for S. typhimurium FljB (SEQ ID NO: 2) are E. coli (SEQ ID NO: 3) and P. aeruginosa ID NO: 4) was in the form of a loop in the predicted secondary structure of Praseline. Thus, with respect to the loop of domain 3 of SEQ ID NO: 2, the predicted loop of domain 3 and the insertion site such as D3I-i1 and D3I-o1 were found in E. coli (SEQ ID NO: 3) and P. aeruginosa (SEQ ID NO: 4) prazoline.

The insertion site in the loop of domain 3 for fusion to the E. coli FliC prazoline (SEQ ID NO: 3) for an antigen with an isoelectric point greater than about 7.0 is β-stranded ITF (amino acid residue 267- 26) and the D3I-o1 site between G274 and A275 of SEQ ID NO: 3 in the loop between the [beta] -string VLTANI (SEQ ID NO: 134, amino acid residues 284-289 of SEQ ID NO: 3) have. The D3I-i1 site is located between the? -Style ELAKLAIKL (SEQ ID NO: 135, amino acid residues 248-256 of SEQ ID NO: 3) and IEYK (SEQ ID NO: 136, amino acid residues 262-265 of SEQ ID NO: 3) Lt; RTI ID = 0.0 &gt; A257 &lt; / RTI &gt; The D3I-s1 site is located in the loop between the β-strand KV (residues 238-239 of SEQ ID NO: 3) and the β-strand SID (residues 243-245 of SEQ ID NO: 3) It was selected between S240 and G241.

P. Ke rugi industrial plastic jelrin (PAO1, SEQ ID NO: 4 ) of the case, D3I-o1 site is β- strand TVSLA (SEQ ID NO: 137, SEQ ID NO: 4 amino acid residues 262-266) and the β- Was selected between Q272 and D273 in a loop between the strand LGITASI (SEQ ID NO: 138, amino acid residues 285-291 of SEQ ID NO: 4). The D3I-i1 site is located between the β-strand SLNFDVTVG (SEQ ID NO: 139, amino acid residues 251-259 of SEQ ID NO: 4) and TVSLA (SEQ ID NO: 137, amino acid residues 262-266 of SEQ ID NO: 4) Lt; RTI ID = 0.0 &gt; S260 &lt; / RTI &gt; The D3I-s1 site is encoded by the SEQ ID (SEQ ID NO: 140, SEQ ID NO: 4 238-241) and the beta-strand GVT (residues 246-248 of SEQ ID NO: 4) NO: 4 between S245 and G246.

Example 2. Fusion protein of influenza B HA antigen in place of domain 3 of prazoline

A composition comprising R3 constructs of Praseline fused to a portion of HA is disclosed (U.S. Patent Application 12 / 905,584). The R3 fusion protein described in the prior art is an influenza A HA antigen (H1, A / Puerto Rico / 8/34, SEQ ID NO: 141), season SI03 (H1, A / Solomon Island / 3/2006, SEQ ID NO : 142, pandemic CA07 (H1, A / California / 07/2009, SEQ ID NO: 143), and IN05 (H5, A / Indonesia / 5/2005, SEQ ID NO: 144) And is immunologically strong (US patent application 12 / 905,584).

However, R3 (SEQ ID NO: 122) fused to the Flu B HA 1-2 moiety bearing the? -Sheet at the bottom of the spherical head, such as B / Florida / 4/2006 (B / FL) of Yamagata Lineage The construct lacked immunogenicity in the mouse model (Fig. 2a). In this study, groups of 5-10 BALB / c mice (female, 6-8 weeks old) were treated with either 10 μg (●) or 3 μg (■) HL098 (SEQ ID NO: 122) or 10 μg (Sc) or intramuscularly (im) immunizations twice (0 day and 21 days) with HL199 (SEQ ID NO: 145) of 3 μg (▼) The HL098 fusion protein is referred to herein as the " R3 construct "and includes a fragmented domain lacking domain 3, replacing domain 3 with HA1-2 (SEQ ID NO: 45). The HL199 fusion protein is referred to herein as the " R23 construct "and includes Praselin lacking domains 2 and 3, replacing domains 2 and 3 with HA1-2 (SEQ ID NO: 45). Mice were collected at 35 days after booster immunization. Serum samples were prepared and stored at -20 ° C until use. Serum antibody titer was measured by hemagglutination inhibition (HAI) assay or micro-neutralization (MN) assay.

The HAI test was used to measure influenza HA specific antibodies in serum samples (Liu, G., et al., PLoS ONE 6 (6): e20928 (2011); Kendal, AP, et al., J. Clin . Microbiol . 18 (4): 930-934 (1983)). In this assay, immune sera samples collected at various times after immunization were treated overnight with receptor-destructive enzyme (RDE) II to remove non-specific hemagglutinin inhibitors. The samples were then heat inactivated (56 ° C., about 30-45 minutes), serial dilution starting at about 1: 5 ratio, incubation with influenza B virus of about 4 HA units (HAU) for about 30 minutes at room temperature . The turkey red blood cells (0.5%) were incubated with the samples for about 30 to about 60 minutes at room temperature. The HAI titers were measured and reported as the inverse of the highest dilution that completely inhibited hemagglutination. Anti-Influenza B virus (from the Centers for Disease Control) Use ferrets after infection as reference sera. Serum HAI antibody titers were measured by HAI assay for B / Florida / 4/06 and plotted as individual values using geometric mean titers (GMT). HL098 (SEQ ID NO: 122) does not induce HAI titer.

The negative control F147 buffer contains 10 mM L-histidine, 150 mM NaCl, 5% trehalose, 0.02% polysorbate 80, 0.1 mM EDTA, 0.5% ethanol, and 10 mM Tris . F147 is a buffer control (♦) and HA0 (○, full-length HA) expressing BV (baculovirus) is used as a positive control. As shown in FIG. 2A, no mice originally produced neutralizing antibodies against the R3 format composition. A reasonable improvement in immunogenicity is achieved by using an alternative fusion protein format designated R23 (HL199, SEQ ID NO: 145) in which the HA1-2 portion (SEQ ID NO: 45) replaces both the D2 and D3 domains Respectively. However, the activity was not sufficient (very low) to provide the composition used in the method for clinical development. In a subsequent study, R23 (HL199; SEQ ID NO: 145) was used as a baseline for comparison to generate novel improved fusion proteins.

The predicted isoelectric point (pI) of a portion of the HA of influenza B (Flu B), for example the HA1-2 portion of the spherical head of Flu B (SEQ ID NO: 45), is about 8.5 to about 9.5, Compared to H1 influenza A at 7.0 or H5 influenza A at a pi of about 8.0. Amounts positively charged at portions of the globular head of influenza B HA (e.g., SEQ ID NOs: 8, 9, 45, and 61) can negatively interact with charge and prazoline at neutral pH. As a result, undesirable charge-charge interactions can distort the fusion protein morphology, which could interfere with the TLR5 signaling by the prazoline component of the fusion protein and the presentation of the antigenic component of the fusion protein. Various efforts to lower the pi of Flu B spherical heads, such as introducing negative amino acid residues in non-antigenic regions, have not been successful. The addition of negatively charged residues to the junction region between HA head and praseline improved TLR5 signaling and fusion protein immunogenicity. For example, the nine amino acid residues with a negative charge (SEQ ID NO: 123) are replaced by HA1-N1 of influenza B (HL352, SEQ ID NO: 125), which naturally contains two negatively charged residues (E306 and D308) When fused to the C-terminus of the two moieties, the immunogenicity of the Flu B fusion protein was moderately improved (Figure 2b). These nine amino acid residues of SEQ ID NO: 123 originate from naturally occurring HA. In another embodiment, additional negatively charged amino acid residues may be added to the portion of the HA, or negatively charged amino acid residues may replace the naturally occurring amino acid residues at the carboxy-terminus of HA.

In this study, sera were tested in a microinfiltration (MN) test (Rowe, T., et al., J. Clin . Microbiol 37: 937-943 (1999); Song, L., et al. PLoS ONE 3: e2257 2008). Briefly, groups of 10 BALB / c mice were sc sc treated at day 0 and 21 with fusion protein compositions containing HL199 (•, SEQ ID NO: 145) or HL352 (•, SEQ ID NO: 126) , And blood was collected on the 35th day. Serum samples were treated with receptor-destructive enzyme II, double-serial dilution starting at a ratio of about 1: 10 and co-incubated with 100 TC _ID50 (tissue culture infectious dose, TCID) of influenza B virus for about 1.5 hr . Madin-Darby dog kidney (MDCK) cells (about 4 x 10 ⁴ / well) were then added and incubated at about 37 ° C for about 20 hours. Cells were washed, fixed, air-dried, incubated with monoclonal anti-influenza B nuclear protein antibody (primary) and goat anti-mouse Fcγ specific IgG: HRP (secondary). Serum antibody titers were measured by MN testing for the B / Florida / 4/06 virus and plotted individually using GMT (Horizon, FIG. 2b). Controls include formulation buffer (+, F147, negative) and HA (*, full-length HA, positive) expressing BV (baculovirus). The negative charge of the linker that fuses the HA moiety to the prazoline can alleviate the charge-charge interaction and allow the plasgelin to bind to TLR5 more efficiently, resulting in an adaptive immune response.

The ability of the fusion proteins described herein to stimulate the innate arms of the immune system, the TLR5 biological activity, was assessed by in vivo TLR5 assays. The assay consists of a lifetime step and in vitro serum cytokine elevation readout. Generally, groups of BALB / c mice (5 per group) were injected with about 1 μg of each vehicle control (inexperienced) or test fusion protein composition, respectively. Three hours later, mice were drawn, serum prepared, analyzed for inflammatory cytokines (BD Biosciences, San Jose, Calif.) Using a mouse blood count bead array (CBA) from BD and run on a flow cytometer .

For cytokine evaluation, only IL-6 and TNF-a showed a range of responses useful for characterizing fusion protein composition candidates, while others only generated baseline levels at selected doses and time points, or the ability of compositional efficacy to stimulate TLR5 activation We generated plateau levels that are not useful for distinction (data not shown). (STF2.HA1-2, B / Florida / 4/2006, SEQ ID NO: 2), which produces minimal innate immune stimulation as well as low micronization (MN) : 146), the activity of zone 4 was established. The active levels of these four zones are shown in Figures 3a and 3b. The lowest level of cytokine activity, designated as inactive, is composed of a level of approximately less than or about + 3 standard deviations (SD) of that detected in inexperienced mice. The next level designated as low is composed of approximately inferior average of inexperience + 3 SD of inexperience and approximately below average or average + 1 SD of low-affinity fusion protein (SEQ ID NO: 146). (A / California / 07/2009, CA07), a high potency fusion protein composition (HL185, STF2R3.HA1-2, R3 constructs) SEQ ID NO: 143) or a value of mean + 3 SD. Finally, the fourth region designated as high is the value of roughly average over + 3 standard deviation (SD) of the highly potent composition.

In vivo TLR5 bioassays were used to evaluate charge-charge interactions that could affect TLR5 binding activity. To a fusion protein comprising the HA1-2 portion of influenza B / Florida / 4/2006 to generate a fusion protein referred to as HL352 (SEQ ID NO: 125), a negatively charged linker of nine amino acids (SEQ ID NO: 123) improved the cytokine response as suggested by the increased IL6 and TNF-alpha responses (Figures 3a and 3b).

Similar results were obtained for fusion proteins using sequences from B / Brisbane / 60/2008 (B / BR) as a circular composition for Victoria Lineage (Figs. 4A and 4B). Figures 4a and 4b show that Balb / c mice remain inexperienced (◆) or that the indicated fusion protein composition for 1 μg dose of B / BR (Victoria Lineage) has been injected: R3.HA1-2 B (▼, HL169 , SEQ ID NO: 147), and R3.HA1-2B (SEQ ID NO: 148) with 9 amino acid linkers. The R3.HA1 (•, HL185, SEQ ID NO: 143) fusion protein was included as a positive control. At 3 hours, mice were bled to generate serum. Cytokine levels were quantitated using mouse infra-red blood count bead arrays (BD Biosciences, San Jose, Calif.). The dashed lines in Figures 4a and 4b represent the activity levels discussed above.

(SEQ ID NO: 149) for B / FL and HL611 (SEQ ID NO: 150 for B / BR) for a total of 5 negatively charged amino acid residue extensions with an additional 3 negatively charged amino acid residues ) At the carboxy-terminus of the portion of HA. The three negatively charged residues originate from naturally occurring HA sequences. For example, the three negatively charged amino acid residue substitutions may be K298E, S300D and I304D in HA B / FL of SEQ ID NO: 124, or K299E, S301D and I305D in HA B / BR60 of SEQ ID NO: . The three negatively charged amino acid residues need not be a continuous stretch of amino acid residues in the naturally occurring HA protein. The negatively charged amino acid residues reduce the charge-charge interaction between the positively charged portion of the HA globular head and the negatively charged prasugin, resulting in a charge-charge intramolecular interaction between the antigen and the fraxelin component of the fusion protein Can be minimized.

The in vivo TLR5 bioassay was carried out using Balb / c mice that remained as inexperienced (1) or were injected with the indicated fusion protein composition in the amount of 1 μg as described above: B / FL (Yamagata Lineage) SEQ ID NO: 123 Additional negative charge (described above, K298E, S300D and I304D in HA B / FL of SEQ ID NO: 125), R3.HA1-2B (I, HL352, SEQ ID NO: 125) with 9 amino acid linkers (HL610, SEQ ID NO: 149) and B / BR (Yamagata Lineage) into which 9 amino acid linkers (SEQ ID NO: 149) and SEQ ID NO: : HL611, SEQ ID NO: 147) and an additional negatively charged amino acid introduced into the linker (HL611, SEQ ID NO: 150). R3.HA1 (•, HL185, SEQ ID NO: 143) was included as a positive control. The dashed lines in Figures 5a and 5b show thresholds of cytokine levels correlated with immunogenicity as described above. The constructs HL610 (SEQ ID NO: 149) and HL611 (SEQ ID NO: 150) improved the cytokine profile compared to constructs HL352 (SEQ ID NO: 125) and HL169 (SEQ ID NO: 147) 5b).

In addition to the in vivo TLR5 cytokine assay used to evaluate the functionality of the prazoline moiety, the neutralization inhibition assay (NIA) was used to assess the efficacy of the HA moiety. NIA was used to test the efficacy of a commercial influenza composition (TIV, Trigger Influenza Vaccine (TIV) containing two different Inactivated Influenza Type A strains and one Inactivated Influenza Type B strain, e.g., FLUVIRIN®) Similar to that used in Single Radial Immunodiffusion, the ability of a fusion protein composition to compete with the virus for binding to a neutralizing antibody present in a positive-immunity serum (available from CBER, Center for Biologics Evaluation and Research in FDA) To assess the integrity of the neutralizing epitope for the fusion proteins described herein.

In the NIA assay, the high efficacy of the fusion protein has been demonstrated by the increased depletion of neutralizing antibodies in the hyperimmune serum, which causes the test virus to infect MDCK cells. Immunoglobulin sera was generated continuously for the positive Flu-B influenza virus (B / Florida / 4/06 serum (FDA) positive anti-HA or B / Brisbane / 60/08 serum (FDA) Pre-incubated with the diluted test article for about 90 minutes at a ratio of about 1: 1. MDCK cells were then added after the addition of 50 TCID ₅₀ B / Florida / 4/06 virus or 50 TCID ₅₀ B / Brisbane / 60/08 virus and incubation at 37 ° C for about 1 hour. After incubating the mixture with MDCK cells at about 37 ° C for about 18 hours to about 20 hours, the cells were incubated with DPBS (1.47 mM KH ₂ PO ₄ , 2.67 mM KCl, 138 mM NaCl, 8.06 mM Na ₂ HPD ₄ .7H ₂ O, Invitrogen Cat. No. 14190-250) in a cold solution of 80% acetone.

The intracellular influenza virus was used as the primary antibody for influenza B NP-specific (nuclear protein-specific) mAb (monoclonal antibody) and horseradish peroxidase (HRP) conjugated goat anti-mouse IgG (Jackson ImmunoResearch, Cat No. 115-035-008) in an enzyme-linked immunosorbent assay (ELISA) format. Virus was quantified by measuring OD ₄₅₀ after color development using TMB (3,3'-5,5'-tetramethylbenzidine) substrate (ThermoScientific, Cat. No. 34028). The NIA curve was generated by Log-Logit fit model using Softmax software 5.2. The greater the integrity of the neutralizing epitope in the composition, the greater the infectivity of the virus and the higher the signal in the NIA assay.

To complement the TLR5 assay, an NIA assay was performed to determine the integrity of the HA antigen in a Flu B composition containing the voice linker (SEQ ID NO: 149 for HL610 and SEQ ID NO: 150 for HL611) Respectively. As shown in Figure 6, the B / Florida / 4 / 06R3 composition of fusion protein HL352 (SEQ ID NO: 125) or HL610 (SEQ ID NO: 149) exhibits a similar ability to inhibit antibody neutralization. As shown in Figure 7, the B / Brisbane / 60/08 R3 composition of the fusion proteins HL169 (SEQ ID NO: 147), HL483 (SEQ ID NO: 148), and HL611 (SEQ ID NO: 150) . These results indicate that the influenza B portion of the HA globular head fused to the loop of domain 3 of the praxelin similarly folds to provide an epitope similar to that of wild-type virus. Given this similarity, additional three tones corresponding to the amino acid residues of the naturally occurring HA, with or without the fusion protein described herein, such as the nine amino acid extension (SEQ ID NO: 123), in triggering TLR5 signaling Differences in the ability of FluB antigens fused to the loop of domain 3 with or without a charged amino acid residue are important in determining fusion protein efficacy.

Example 3. A fusion protein with an HA antigen inserted into the loop region of domain 1, 2, or 3 of the flagellin for targeting influenza B by transferring pI

Negative charge in the linker region improved TLR5 signaling, but the immunogenicity of such fusion proteins (SEQ ID NOs: 149 and 150) remains lagging behind Victoria Lineage, especially B / BR. The voice linker can only localize the orientation of the HA head relative to the flagellin, which may not be sufficient to allow the formation of a 2: 2 heterodimer that is critical to initiating the TLR5 signaling chain reaction. As disclosed below, the portion of the HA bulbous head was further orientated away from domain 1 of the TLR5 binding domain, pravastatin. For example, as shown in FIG. 14, domain 1 of S. typhiurium FliC prazilin has amino acid residues 47-176 (amino-domain 0) of SEQ ID NO: 2 and amino acid residue 415 of SEQ ID NO: 2 -464 (carboxy-domain 0). Fusion protein constructs (HL656, SEQ ID NO: 151, D3Ins and HL657 of B / FL, D3Ins of SEQ ID NO: 128, B / BR) fused a portion of the globular head of the HA antigen to domain 3 of the labassin , Which is referred to as the domain 3 insert ("D3Ins").

As shown in Figures 8a and 8b, more favorable cytokine profiles were observed using D3Ins fusion protein as assessed by in vivo TLR5 assays. As described above, Balb / c mice remained in inexperienced () or were injected with an indicated composition candidate of about 1 μg dose: B / FL (Yamagata Lineage) R3.HA B (1, HL352, SEQ ID NO: 125 ) And D3Ins.HA B (▲, HL656, SEQ ID NO: 151), B / BR (Victoria Lineage) R3.HA B (▲, HL169, SEQ ID NO: SEQ ID NO: 128). R3.HA1 (•, HL185, SEQ ID NO: 143) was included as a positive control. The fusion protein produced by the removal of domain 3 of the prazoline and substitution as part of the HA globular head, referred to as the "R3" fusion protein (e. G. R3.HAB) / 905,584). The NIA assay did not detect a detectable difference between the D3Ins fusion protein and the R3 fusion protein, indicating that the antigen retained similar integrity in both the stones (Figures 9a-9c). The NIA assay evaluates the functionality of the portion of the spherical head of the HA.

NIA assays were performed using an approximately 1: 1 ratio mixed with both anti-HA of B / Florida / 4/06 serum (A), B / Brisbane / 60/08 (B), or B / Wisconsin / (HL352, SEQ ID NO: 125 and?, HL656, SEQ ID NO: 151) (Fig. 9A) of the continuous diluted test article B / Florida / 4/06; B / Brisbane / 60/08 (□, HL611, SEQ ID NO: 150 and ○, HL657, SEQ ID NO: 128) (FIG. Or B / Wisconsin / l / 10 (▲, HL724, SEQ ID NO: 152 and o, HL772, SEQ ID NO: 126) (Fig. 9c). TLR5 signaling is believed to play a more important role in inducing protective immune responses than neutralization inhibition. When the mouse is immunized with the D3Ins fusion protein, HL610 (SEQ ID NO: 149) (O, R3 fusion protein with a negatively charged amino acid (SEQ ID NO: 153) with 9 amino acid extensions) and HL656 (SEQ ID NO: 151) (O, D3Ins (SEQ ID NO: 123) with 9 amino acid extensions) is HL352 (SEQ ID NO: 125) Lt; RTI ID = 0.0 &gt; R3) &lt; / RTI &gt; with extended portions (Figure 10). HA352 (SEQ ID NO: 125) is an R3 fusion protein comprising the HA1-2 portion of the globular head of influenza B FL4. The serum antibody level of Figure 10 was measured by the MN test using the B / Florida / 4/06 viral antigen. Data are presented as the serum conversion of each of the above groups (percent (%) of mice with MN titer ≥ 80) and the titer of individual mice to GMT. This data indicates that the D3Ins format (HL656, SEQ ID NO: 151) was superior to the R3 format for Flu B (HL352, SEQ ID NO: 125).

The immunogenicity of the D3Ins fusion proteins listed in Table 3 was evaluated using the recently circulating Yamagata Lineage strain B / Wisconsin / 1/2010. In an immunogenicity study, groups of six BALB / c mice were injected with s.c. in two injections on days 0 and 21 using the Flu B composition. Was injected with a fusion protein of three different formats, including a portion of the globular head of HA of influenza B delivered at 6 μg volume of HLA, and the conjugated protein: R3 B / WI (•, HL719, SEQ ID NO: 154, (R3 with additional negative charge in the linker), D3Ins B WI (▲, HL772, SEQ ID NO: 126), or F147 buffer (●). Mice were bled at 35 days for HAI titers. Controls included groups immunized with F147 buffer (10 mM L-histidine, 150 mM NaCl, 5% trehalose, 0.02% polysorbate 80, 0.1 mM EDTA, 0.5% ethanol, 10 mM Tris, pH 7.2). All fusion proteins were prepared in F147 buffer. Serum was tested by HAI assay using extracted B / Wisconsin / 1/2010 virus antigen. Data are presented as titers of individual mice using GMT. Statistical differences were measured by 1-way ANOVA / Tukey test. *, p < 0.05, ***, p < 0.001.

As illustrated in FIG. 11, the highest inverted group in the monovalent group was the D3Ins fusion protein (HL772, ▲, SEQ ID NO: 126) followed by the R3 fusion protein HL724 (SEQ ID NO: 152, B / FL HL610 B / WI counterpart, SEQ ID NO: 149) and HL719 (SEQ ID NO: 154, B / WI counterpart of B / FL HL352, SEQ ID NO: 125). The potency of both the HL724 (R3 format) and HL772 (D3Ins format) groups was significantly higher than the F147 control. This was in accordance with the same format of B Florida and B Brisbane, where D3Ins was the highest followed by the R3 format (Figure 10 for B / FL, B for Victoria Lineage including Brisbane, Hong Kong and Bangladesh). Thus, as predicted by TLR5 data, the D3Ins format improved immunogenicity against the B / WI strain compared to the R3 format for fusion proteins in mice. A positive immunization control was not included because the immunogen for B / Wisconsin / 1/10 was not available at the time of analysis.

The HAI assay of immunized sera from mouse immunogenicity studies comparing the R3 and D3Ins formats of B Brisbane-like strains was performed. HA antigen (SEQ ID NOS: 95-97), and these antigens were used for the R3 and D3Ins formats. Groups of 6 BALB / c were immunized with 6 μg of the fusion protein R3 composition (HL611, SEQ ID NO: 150; HL753, SEQ ID NO: 155; HL742, SEQ ID NO: 156) or B / Brisbane / 60/08-like virus (B / Brisbane / 60/08 or B / BR, HL657, SEQ ID NO: 128; B / Hong Kong / 259/10 or B / HK, HL774, SEQ ID NO: 157; B / Bangladesh / 5945/09 or B / BD, HL787, SEQ ID NO: 158) Immunized and blood was collected on the 35th day. Control mice received 15 μg of FLUVIRIN® or F147 buffer. The neutralizing antibody titers of the serum samples were determined by HAI assay using extracted B / Brisbane / 60/08, B / Hong Kong / 259/10, or B / Bangladesh / 5945/09 viruses and expressed as GMT. Statistical differences were measured by 2-way ANOVA / Tukey test. *, p < 0.05, **, p < 0.01.

The results of this study showed that the B / Brisbane / 60/2008-like fusion protein (B / Brisbane / 60/08, B / BR SEQ ID NO: 128; B / Hong Kong / 259/10, 157 and B / Bangladesh / 5495/09, B / BD SEQ ID NO: 158) resulted in significantly higher HAI titers than the strain-matching R3 format measured using three different B / Brisbane-like viruses (Fig. 12). D3Ins B / BD (HL787, SEQ ID NO: 158) induced HAI geometric mean titers comparable to FLUVIRIN® containing B Brisbane, particularly when the B / Hong Kong and B / Bangladesh viruses were used as HAI antigens . These data indicate that the D3Ins fusion protein consistently inhibits hemagglutininization over a number of influenza B strains and in a cluster of antigenically similar viruses than the R3 fusion protein. The fusion protein comprising the part of the globular head of influenza B fused to the loop of domain 3 of the praxelin improved immunogenicity compared to the HA moiety fused to the R3 construct.

Example 4. Screening of Insert Mutants as Flu B Fusion Proteins

The initial design of the insert fusion protein targeted the D3 domain as the insertion site. Three insertion sites (D3I-o1, D3I-i1 and D3I-s1) in the loop of domain 3 were selected for fusion of portions of the HA antigen (see, e.g., Figures 29 and 30). (B / WI, SEQ ID NO: 263), which is currently circulating the B Yamagata lineage, in addition to the B / FL fusion protein of the seasonal Flu B fusion protein used in the method of stimulating the immune response Selected for development. B / BR remains another candidate in the development of fusion proteins representing another circulating B-Victoria Lineage Flu B strain. Three constructs (HL772, D3I-o1, SEQ ID NO: 126; HL849, D3I-i1, SEQ ID NO: 159 and HL848, D3I-s1, SEQ ID NO: 160) of B / , And the protein was purified from E. coli cell culture medium using standard fermentation as previously described (Song, L., et al., PLoS One 3: e2257 (2008); Song, L., et al. , Vaccine 27: 5875-5884 (2009)).

The TNF-alpha and IL-6 cytokine levels of the B / WI construct are shown in Figures 13a and 13b. H1 CA07 R3.HA1 (also referred to as HL185, "VAX128", SEQ ID NO: 143) The R3 format of the fusion protein was used as a positive control. The CA07 vaccine R3.HA1 (HL185, SEQ ID NO: 143) fusion protein is safe and immunogenic in humans (Taylor, D., et al., Vaccine 30: 5761-5769 Positive control group induced high levels of TNF-a and IL-6.

A fusion protein comprising the HA antigen fused to the loop of domain 3, B Wisconsin (Yamagata Lineage), including HL772 (D3I-o1, SEQ ID NO: 126) and HL849 (D3I- Induced a comparable level of IL-6 in the "high" region when using HL848 (D3I-s1, SEQ ID NO: 160), the lowest in the "intermediate" The TNF-alpha levels for HL772 (D3I-o1, SEQ ID NO: 126) and HL849 (D3I-i1, SEQ ID NO: 159) were lower than for the positive control, but the minimum threshold required to achieve an appropriate immune response . The fusion protein HL848 (D3I-s1, SEQ ID NO: 160) has TLR5 activity in the "inactive" region indicating that the D3I-s1 format may not induce a potent immune response (Figs. 13A and 13B). This data suggests that a fusion protein comprising an antigen fused to the loop of domain 3 of the praxelin has less side effects (less reactive) than a fusion protein comprising an antigen fused to the R3 construct of praxelin, Lt; RTI ID = 0.0 &gt; cytokine &lt; / RTI &gt; See Tables 1, 3 and 4 for a listing of fusion sites and insertion sites of the fraxelin.

For evaluation of fusion proteins maximizing TLR5 signaling and immunogenicity while minimizing adverse effects, loops of domain 2 and domain 1 plaslane in addition to the loop of domain 3 of prazoline were selected as possible fusion sites for the antigen. Since the insertion (fusion) site of the prazoline is located in the loop region, the HA antigen could be inserted without interfering with the overall Phrazzelian structure including the tertiary structure of domain 3 of Praseline shown in Figs. 14 and 29. The primary amino acid sequence of the flagellin, representing the amino acid residues of prazoline in which the parts of the bulbous head of HA from influenza B are fused, is shown in Figures 29 and 30. The predicted loop in the domain of prazoline is based on a comparison of the known tertiary structure of S. typhimurium FliC prazoline as discussed above. Exemplary fusion proteins of the invention include Yamagata Lineage B / Wisconsin / 1/2010 listed in Table 3, and Victoria Lineage B / Brisbane / 60/2008 listed in Table 4.

Table 3. Flu B Yamagata Lineage (B / Wisconsin / 1/2010) Fusion protein. The fusion protein comprises a portion of the globular head (SEQ ID NO: 50) of HA fused to the loop of the domain of S. typhimurium FljB pregulin (SEQ ID NO: 2 or 127).

Table 3

Table 4. Flu B Victoria Lineage (B / Brisbane60 / 2008) Fusion protein. The fusion protein comprises a portion of the globular head of HA (SEQ ID NO: 48) fused to the domain of S. typhimurium FljB pregulin (SEQ ID NO: 2, 127, or 270).

Table 4

The fusion proteins listed in Tables 3 and 4 were evaluated using the TLR5 assay as described above. Comparisons of fusion proteins inserted (D3I) into domain 3 of prasugline compared to insertion (D2I) of domain of prazoline into domain 2 are shown in Figures 15a-15b and 16a-16b. The fusion protein constructs used were the following: B Wisconsin (Yamagata Lineage) D3I-o1 (HL772, SEQ ID NO: 126), D2I-o1 (HL825, SEQ ID NO: 161), D2I- ), D2I-o3 (HL827, SEQ ID NO: 163), D1I-o1 (HL828, SEQ ID NO: 164) and D2I-i1 (HL850, SEQ ID NO: 165) and B Brisbane (Victoria Lineage) D3I-o1 (HL657, SEQ ID NO: 128), D2I-o1 (HL733, SEQ ID NO: 166), D2I-o1 (HL856, SEQ ID NO: 167) and D2I-o2 15a-15b). The fusion protein constructs used were D3I-o1 (HL772, SEQ ID NO: 126), D3I-o2 (HL888, SEQ ID NO: 169), D2I-cl (HL890, SEQ ID NO: 169), B Wisconsin (Yamagata Lineage, (HL858, SEQ ID NO: 170), D2I-i2 (HL892, SEQ ID NO: 171) and B Brisbane (Victoria Lineage, 172), D3I-s1 (HL860, SEQ ID NO: 173), D3I-o2 (HL889, SEQ ID NO: 174), D2I- NO: 176). R3.HA1 (HL185, SEQ ID NO: 143) was included as a positive control.

This data shows that fusion proteins ("D3 insertion constructs", "D3I", "D3Ins", "D3Ins fusion proteins") containing antigens fused to the loop of domain 3 of praslin ("D2 insertion construct") comprising a fusion antigen. The fusion protein ("D1 insert construct") containing antigens fused to the loop of domain 1 of prazoline was not active. Among the D3Ins fusion proteins, D3I-o1 (HL772, SEQ ID NO: 21) and D3I-i1 (HL849, SEQ ID NO: 22) were more active than D3I-s1 (HL848, SEQ ID NO: -16).

Antibodies that generate fusion proteins bearing portions of globular heads fused to domain 3, domain 2, or domain 1 were compared for their ability to inhibit virus neutralization in NIA assays. NIA assay data for antibodies that generate fusion proteins are compared with the R3 format (▲, HL724, SEQ ID NO: 152): D3Ins (O, HL772, D3I-o1, SEQ SEQ ID NO: 126), HL827, D2I-o3, SEQ ID NO: 163, HL826, D2I-o2, ), And D1Ins (1, HL828, D1I-o1, SEQ ID NO: 164), which are shown in FIG. The NIA assay data for the D3I-inserted fusion protein relative to the D2I-inserted fusion protein is shown in FIG. The portion of the globular head fused to the loop of domain 2 or the loop of domain 3 has the same amino acid sequence (SEQ ID NO: 50).

18A shows the B / Wisconsin / 1/2010 D3I insertion mutant: D3I-o1 (SEQ ID NO: 165) as compared to the fusion protein D2I-i1 (•, HL850, SEQ ID NO: 165) and D2I Hl864, SEQ ID NO: 126), D3I-s1 (?, HL848, SEQ ID NO: 160), D3I-i1 (?, HL849, SEQ ID NO: NO: 177). &Lt; / RTI &gt; 18A is a B / Wisconsin / 1/2010 D3I mutant: D3I-o1 (O, HL772, SEQ ID NO: 126), D3I-o2 (□) compared to D2I-i2 (◇, HL892, SEQ ID NO: , HL888, SEQ ID NO: 169), and D2I-cl (Δ, HL890, SEQ ID NO: 170).

A relatively high NIA regulator was observed with the D3 insert fusion protein as compared to the R3 format, as demonstrated by comparing HL772 (O, D3Ins, SEQ ID NO: 126) with HL724 (▲, R3, SEQ ID NO: 152) Exhibits slightly better antigen presentation to the D3 insertion format than the R3 format. The NIA regulator indicates that fusion of antigens to prazoline can deplete serum neutralizing antibodies, which may not be related to the ability of the fusion protein to produce a protective immune response. The ability to generate a protective immune response involves balancing the ability of the fusion protein to activate TLR5 and stimulate a sufficient immune response with minimal side effects.

The advantage of fusing the antigen to the loop of domain 3 of the praxelin by inducing important cytokine secretion in response to immunization is shown in Figures 9a-9c. Taken together, the cytokine and NIA results indicated that the D3 insertion format of prazoline was a better format for fusing parts of the bulbous head of influenza B than the R3 format. Furthermore, the D3-inserted fusion protein showed higher neutralizing antibody titers than the D2-inserted fusion protein. Consistent with cytokine assays, the D1 insert fusion protein was inactive in the NIA assay. Among the three D3-inserted fusion proteins, D3I-o1 and D3I-i1 also showed greater capacity to neutralize viral infection than D3I-s1. NIA data are consistent with cytokine activation to assess TLR5 activation.

BIA / Brisbane / 60/2008 was used as a circle to assess the fusion protein containing the part of the globular head of influenza B against Flu B Victoria Lineage. (D3I-o1 (O, HL657, SEQ ID NO: 128) and D3I-i1 (HL861, SEQ ID NO: 180) as compared to the fusion protein: R3 (?, HL611, SEQ ID NO: Lt; RTI ID = 0.0 &gt; 19A. &Lt; / RTI &gt; Figure 19b shows that the part of the spherical head is different fusion protein D3I-o1 (O, HL657, SEQ ID NO: 128), D2I-o1 (?, HL733, SEQ ID NO: 166), D2I-o1 (HL856, SEQ ID NO: 167), D2I-o2 (▲, HL857, SEQ ID NO: 168), and D2I-i1 NIA assay data for B / Brisbane / 60/2008 R3 (□, HL611, SEQ ID NO: 150) fusion protein. D2I fusion protein: D3I-s1 (?, HL860, SEQ ID NO: 173), D3I-o2 (HL889, SEQ ID NO: 174), D2I- (SEQ ID NO: 176), and D2I-i1 (HL862, SEQ ID NO: 181), and D2I-o3 (?, HL858 , SEQ ID NO: 172) is shown in FIG.

As shown in Figure 19 (a), the D3Ins fusion protein was comparable to the R3 fusion protein in neutralization inhibition and showed similar integrity in both fusion protein formats. When evaluating in vivo cytokine data for the TLR5 test, it was found that the R3-format fusion protein of B / Brisbane / 60/2008 was an insufficient promoter of cytokine release, which is considered to be an important event inducing an adaptive immune response. Thus, the D3Ins fusion protein is an exemplary format for Flu B Victoria Lineage.

As shown in Fig. 19B, the D2Ins fusion proteins were similar and generated somewhat lower activity than the D3Ins fusion protein. However, the TLR5 activity of the D2Ins fusion protein construct was significantly lower than the D3Ins fusion protein (Figures 15a, 15b, and 16b). As a result, D3Ins fusion proteins such as HL657 (D3I-o1, SEQ ID NO: 128) and HL861 (D3I-i1, SEQ ID NO: 180) are considered to be better for the method of stimulating the immune response.

In conclusion, the fusion of antigens ("D3Ins fusion protein") with an isoelectric point of greater than about 7.0 to the loop of domain 3 of prasugin can significantly improve TLR5 biological activity compared to the R3 format. In NIA functional assays, the D3Ins fusion protein also exhibited equivalent or greater activity to compete with the virus for neutralizing antibodies. The D3 insertion format is suitable, for example, in a fusion protein format used to fuse portions of the globular head of HA influenza B to pravastatin and has an isoelectric point greater than about 7.0, such as about 7.5, about 8.0 or about 8.5, about 9.0, About 9.5, about 10.5, or about 11.0, or better than the R3 or D2Ins format for use with influenza A antigens of influenza B.

Example 5. Immunogenicity of a fusion protein with an HA antigen inserted into the loop region of domain 3 of the flagellin for targeting influenza B by transferring pI in a mouse model

The immunogenicity of the three different fusion proteins inserted in three different regions of the loop of domain 3 was evaluated in mice. Such fusion proteins include D3I-o1, HL772 (SEQ ID NO: 126), D3I-i1, HL849 (SEQ ID NO: 159), and D2I-i1, HL850 (SEQ ID NO: 165). Groups of 8 BALB / c mice were treated with two dose levels (3 μg and 12 μg) of D3I-o1 B / WI (HL772, SEQ ID NO: 126), D3I-i1 B / WI (HL849, SEQ ID NO: 159) and D2I-i1B / WI (HL850, SEQ ID NO: 165) fusion protein at day 0 and im Respectively. On day 35, all mice were bled. Serum HAI antibody was measured by HAI test using the ether-extracted B / Wisconsin / 1/2010 virus. In FIG. 21A, the horizontal line represents the geometric mean titer (GMT) (GMT value above the line). Serum conversion (% of mice representing HAI? 40) was also presented as a percentage in Figure 21a. Statistical differences were determined for the F147 buffer control in the ANOVA test ***, p <0.001.

As shown in FIG. 21A, D3I-o1 B / WI induced about two-fold higher HAI antibody titer than D3I-i1 B / WI. Inactivated virus antigen (B / Wisconsin / 1/2010-like virus obtained from CBER, 6 μg HA HU in FIG. 21a) of B / Hubei-Wujiagang / 158/2009 was used as a positive control, Titer was induced. In contrast, D2I-i1 B / WI (HL850) and baculovirus-expressed rHA0 from Protein Sciences induced significantly lower HAI titers. Buffer F147 was used as a negative control (Fig. 21A). Thus, the immunogenicity of the three B / Wisconsin / 1/2010 fusion proteins was aligned with D3I-o1> D3I-i1> D2I-i1, consistent with the results from cytokine testing and NIA assays.

The D3Ins fusion protein of B / Sichuan / 379/1999 (B Yamagata Lineage, included in 2001/2002 TIV and B / Florida / 4/2006 (2008/2009 TIV)) was also tested for immunogenicity Respectively. Groups of 10 mice were divided into three different doses (0.05 μg, 0.5 μg and 5 μg) of B / Sichuan / 379/1999 D3I-o1 (HL863, SEQ ID NO: 182) or D3I- : 183) Fused protein at 0 day and 21 days sc Immunized. As shown in Fig. 21B, the D3Ins fusion protein of B / Sichuan / 379/1999 had immunogenicity with no statistically significant difference between the o1 or i1 formats. Generally, D3Ins was more immunogenic than D2Ins constructs.

Example 6. D3Ins fusion protein format

In order to confirm the general availability of the D3Ins format of Prazoline used to generate fusion proteins of parts of the globular head of influenza B, fusion proteins for the three circulating strains currently circulating in Yamagata Lineage were evaluated in mouse immunogenicity studies . In this study, the treatment of a group of 8 BALB / c mice was performed as described in B / Wisconsin / 1/2010 (D3Ins B / WI, HL772, SEQ ID NO: 126); B / Hubei-Wujiagang / 158/2009 (D3Ins B / HU HL869, SEQ ID NO: 184); (3 μg and 12 μg) of the fusion protein produced with the HA sequence from B / Texas / 6/2011 (D3Ins B / TX, HL871, SEQ ID NO: 185). HL869 comprises a portion of HA of SEQ ID NO: 58. HL871 comprises a portion of HA of SEQ ID NO: 60.

As shown in Figure 22, the three strain D3Ins fusion proteins induced significant HAI titers (GMT = 71-283 in the 3 [mu] g dose group and 273-719 in the 12 [mu] g dose group). Furthermore, the 3 μg dose of D3Ins B / WI was 12 times more potent than the baculovirus-expressed full-length Wisconsin HA (rHA, HA0 WI, Protein Sciences Corporation, Meriden, CT) at 6 μg dose (GMT = 23, SC = High geometric mean HAI titers (GMT = 283) and higher serum conversion (100%). Thus, the D3 insert-format fusion protein comprising part of the globular head of influenza B Wisconsin (SEQ ID NO: 126) was more immunogenic in mice than rHA WI (Protein Sciences) and was inactivated by the inactivated B / HB virus antigen ).

A number of Victorian Lineage strains were also evaluated. In particular, we assessed the Brisbane-like strain recommended as a 2009-2011 H1N1 influenza vaccine and recommended as a Saga influenza vaccine in 2013-14. As the improved efficacy of the B Brisbane-like strain B / Bangladesh / 5945/2009 in mice has been previously demonstrated, the immunogenicity of the Victorian round fusion protein has been evaluated in rabbit models. Six New NZW (New Zealand White) rabbits (3 of each sex) were infected with Brisbane 60/2008 (SEQ ID NO: 264) or B / Bangladesh / 5945/2009 (SEQ ID NO: 265) (6 μg, 12 μg, and 15 μg) of the fusion protein containing the antigen fused to the loop of im Respectively. FLUVIRIN® 2011-12 (TIV, total 15 μg) was included as a positive immunogenicity control and F147 buffer was included as a negative control. The HAI titer was run with the ether-extracted virus matched to the composition: CBER B / Brisbane / 60/2008 1: 5,120 or ferret B / Bangladesh / 5945/2009 1: 10,240. Data were displayed as bars as the titres of individual rabbits.

The horizon represents the geometric mean titer (GMT value in excess) and the seroconversion rate is given in FIG. As shown in Figure 23, the Bangladesh fusion protein (HL787, SEQ ID NO: 158) was more immunogenic than the Brisbane fusion protein (HL657, SEQ ID NO: 128) at 100% serum conversion when tested with matched virus . Brisbane-like Bangladesh strains (D3Ins B / BR-like) as candidates for Victoria Lineage may be useful in methods of providing protective immunity.

Fusion proteins of antigens fused to the loop of domain 3 were further evaluated for suitability over at least three recent and historical strains. Consistent with this strategy, a trial of historical B candidates was performed using the D3Ins format of B / Sichuan / 379/1999, a historical flu B virus (Yamagata Lineage, STF2D3Ins B / SI, HL863, SEQ ID NO: 182). The portion of the HA fused to the D3-o1 site (see loop 6 in Figures 29 and 30) is SEQ ID NO: 56. B / Sichuan / 379/1999 HAI test of mouse immunity sera against virus was performed. In this experiment, groups of 10 BALB / c mice were treated with a 6 ug dose of STF2D3InsB / SI (HL903, SEQ ID NO: 183) fusion protein or formulation buffer (F147) twice daily at 0 and 21 days. Respectively. On day 35, mice were bled. Serum HAI antibodies were measured using the ether-extracted B / Sichuan / 379/1999 virus and the values were individually plotted using the indicated serum conversion and GMT. The immunogenicity results in Figure 24 showed that the D3Ins composition of B Sichuan (SEQ ID NO: 182) at a dose of 6 μg induced a GMT of 132 with a serum conversion of 100%. These data indicate that D3Ins is suitable for use in generating a composition comprising a portion of the bulbous head of Influenza B and a fusion protein of prazoline that is used in a method of treating seasonal exposure to influenza.

Example 7. Efficacy of a fusion protein with an HA antigen inserted in the loop region of domain 3 of the flagellin to target influenza B by transferring pI in mice

In addition to the immunogenicity tests of the B3 / Sichuan / 379/99 (D3Ins B / SI, HL863, SEQ ID NO: 182, Yamagata Lineage) described above, D3Ins fusion protein of historical B viruses, efficacy studies in a fatal mouse challenge model . Groups of 10 BALB / c mice were immunized with D3Ins B / SI 99 (HL863, SEQ ID NO: 182) fusion protein or F147 buffer control of indicated doses (0.05 μg, 0.5 μg, and 5 μg) , And blood was collected at 35 days. At day 42, mice were challenged intranasally with 5 x LD ₅₀ B / Sichuan / 379/1999 10 ⁵ pfu per mouse, and mortality for 21 days and weight change over 14 days were monitored daily.

Survival and body weight (average percentage of initial body weight) were plotted in Figures 25a-25b. Fusion protein D3Ins B / SI compositions (each immunized twice) at a dose of about 5 μg and about 0.5 μg were tested for 100% survival and less than about 12% weight loss in mice challenged with lethal B / Sichuan / 379/99 virus (Figs. 25A and 25B). In contrast, the placebo group exhibited a survival rate of about 20% and a weight loss of about 75% or about 75%. These results indicated that the D3Ins fusion protein composition of B / Sichuan / 379/99 was effective at doses of less than micrograms. Thus, the efficacy of D3Ins B / SI in such studies supported the general suitability of the D3Ins format used in compositions containing portions of influenza B.

Example 8. Immunogenicity and safety of a fusion protein with an HA antigen inserted in the loop region of domain 3 of the flagellin for targeting influenza B by transferring pI in a rabbit model

The immunogenicity of the D3Ins fusion protein was also evaluated in the rabbit model. A rabbit study was designed to evaluate the immunogenicity of the R3 and D3Ins formats of B / WI at various doses. HAI titers induced by the R3 and D3Ins formats of B Wisconsin in rabbits were measured. 6, 12 and 18 μg of the fusion protein R3B Wisconsin (HL724, SEQ ID NO: 152) and D3Ins B Wisconsin (HL772, SEQ ID NO: 126, D3I-o1 inserion, see Table 1) (Covance Research Products, Denver, Pa.) In a group of 6 New Zealand White rabbits consisting of 3 rats. For this study, the fusion protein was incubated at 0 &lt; RTI ID = 0.0 &gt; And sera were collected at 35 days for HAI analysis. A blend of baculovirus-produced HA or egg-produced inactivated virus (5 μg each) was included as a positive control to match the strain, and F147 buffer was included as a negative control. HAI titers were performed with the ether-extracted B / Wisconsin / 1/210 virus.

Data are plotted as individual rabbit titers and values were individually plotted with the indicated GMT and serum conversion rates (FIG. 26). One of the objectives of the study was to confirm that the D3Ins fusion protein format (HL772, SEQ ID NO: 126) of B / WI is superior to the R3 format (HL724, SEQ ID NO: 152). As shown in FIG. 26, the fusion protein R 3 format induced a low HAI titer and achieved a high serum conversion (about 67%) with a GMT of about 22 at only 18 μg. In contrast, the fusion protein D3Ins format has a maximal response (approximately 83%) to 12 μg and produced approximately 50% or greater serum conversion at all three doses. These results confirmed previous mouse results demonstrating superiority of the D3Ins format. HL772 (SEQ ID NO: 126) may be useful in methods of treating a subject to provide protective immunity.

A dose-range study with D3Ins B / WI (HL772, SEQ ID NO: 126) was performed to establish a suitable dose range for the rabbit model on safety and immunogenicity. A group of 10 NZW rabbits (5 of each sex) were inoculated with STF2D3Ins B / WI (HL772, SEQ ID NO: 126) fusion (3 μg, 6 μg, 9 μg, 12 μg, 15 μg and 18 μg) Protein, inactivated B / Hubei-Wujiagang / 158/2009 virus (5 μg Hubei virus, CBER), or formulation buffer (F147) And blood was collected at 35 days. Serum HAI antibodies were measured by HAI assay using an ether-extracted B / Wisconsin / 1/2010 virus and plotted individually using GMT and serum conversion.

The immunity potential results are shown in Fig. Similar to the mouse results, strong HAI titers were induced by low to moderate microgram doses, with 100% serum conversion occurring at doses as low as about 6 μg. The high potency observed in these studies was probably the result of high purity protein preparations. These results demonstrate that strong influenza B titer can be observed with a low dose of D3-inserted fusion protein comprising the influenza B antigen of the multivalent mixture, thus providing a protective immunity against disease-causing organisms, Lt; RTI ID = 0.0 &gt; and / or &lt; / RTI &gt; low total dose for multivalent blends for compositions that can be used in methods to stimulate the immune response to &lt; RTI ID = 0.0 &gt;

The reactivity of the D3Ins fusion protein was investigated in a rabbit safety model using the previously described technique (Taylor, DN, et al., Vaccine 30: 5761-5769 (2012)). In these models, three measures are found to predispose to adverse events in humans: anorexia (low feed consumption) within 24 hours of initial immunization, increased body temperature after 6 hours of initial immunization, and elevated serum after 24 hours of initial immunization CRP.

(3 mu g, 6 &lt; RTI ID = 0.0 &gt; pg), &lt; / RTI &gt; which is fused to a loop of the domain 3 (HL772, SEQ ID NO: 126) with a formula buffer control (F147) as negative control or an antigen with an isoelectric point of at least about 7.5 (B / Wisconsin / 2010) 9 μg, 12 μg, 15 μg, and 18 μg), respectively. It was measured about 24 hours after immunization of feed consumption (Fig. 28A). The temperature was measured rectally 6 hours after immunization (Fig. 28b). CRP was measured from the serum 24 hours after the initial immunization (Fig. 28C). Data from all measurements are shown as a result of individual rabbits using lines representing mean and standard error of the mean. The dotted line represents the safety threshold calculated using data from the formula control rabbit. Safety thresholds for each of the three scales were derived using averages of formulated control animals from multiple studies and using confidence intervals or multiple standard deviations. In these studies, various doses of fusion proteins (Figures 29 and 30) were fused to loop 6 of Wisconsin influenza B antigen in the domain 3 of the praxelin.

The results indicate that the highest dose of B Wisconsin (D3Ins B Wisconsin, HL772, SEQ ID NO: 126) was safe to a dose of about 18 μg. A dose of about 3 to about 18 [mu] g caused little reduction in feed consumption (Fig. 28A), and all group averages were within safe thresholds. Similarly, the rise in temperature at about 6 hours was minimal over the dose range tested (Fig. 28b) and all values were below the safety threshold. Finally, serum CRP at about 24 hours showed only a minor increase below about 18 μg (FIG. 28c). A dose of B Wisconsin D3Ins as high as about 18 μg is suitable as an influenza B component in a multivalent blend that can be used in an immune response against influenza B, particularly a disease outcome or a method of stimulating a protective immune response associated with influenza B infection (I. E., Secure). &Lt; / RTI &gt;

The teachings of all patents, published applications and references cited herein are incorporated by reference in their entirety.

While the invention has been particularly shown and described with reference to exemplary embodiments thereof, it will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the scope of the invention as set forth in the appended claims.

                                SEQUENCE LISTING <110> VaxInnate Corporation       Song, Langzhou       Liu, Ge       Umlauf, Scott       Kavita, Uma       Li, Hong       Liu, Xiangyu       Weaver, Bruce       Tussey, Lynda <120> FUSION PROTEINS AND METHODS OF USE    <130> 3710.1054002 <150> US 13 / 931,028 <151> 2013-06-28 &Lt; 150 > US 61 / 743,165 <151> 2012-08-28 <160> 288 <170> FastSEQ for Windows Version 4.0 <210> 1 <211> 494 <212> PRT <213> Salmonella typhimurium <400> 1 Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn Asn  1 5 10 15 Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu Ser             20 25 30 Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln Ala         35 40 45 Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala Ser     50 55 60 Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly Ala 65 70 75 80 Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala Val                 85 90 95 Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile Gln             100 105 110 Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly Gln         115 120 125 Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu Thr     130 135 140 Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu Lys 145 150 155 160 Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Thr Leu Asn Val Gln Gln                 165 170 175 Lys Tyr Lys Val Ser Asp Thr Ala Ala Thr Val Thr Gly Tyr Ala Asp             180 185 190 Thr Ile Ala Leu Asp Asn Ser Thr Phe Lys Ala Ser Ala Thr Gly         195 200 205 Leu Gly Gly Thr Asp Gln Lys Ile Asp Gly Asp Leu Lys Phe Asp Asp     210 215 220 Thr Thr Gly Lys Tyr Tyr Ala Lys Val Thr Val Thr Gly Gly Thr Gly 225 230 235 240 Lys Asp Gly Tyr Tyr Glu Val Ser Val Asp Lys Thr Asn Gly Glu Val                 245 250 255 Thr Leu Ala Gly Gly Ala Thr Ser Pro Leu Thr Gly Gly Leu Pro Ala             260 265 270 Thr Ala Thr Glu Asp Val Lys Asn Val Gln Val Ala Asn Ala Asp Leu         275 280 285 Thr Glu Ala Lys Ala Ala Leu Thr Ala Ala Gly Val Thr Gly Thr Ala     290 295 300 Ser Val Val Lys Met Ser Tyr Thr Asp Asn Asn Gly Lys Thr Ile Asp 305 310 315 320 Gly Gly Leu Ala Val Lys Val Gly Asp Asp Tyr Tyr Ser Ala Thr Gln                 325 330 335 Asn Lys Asp Gly Ser Ile Ser Ile Asn Thr Thr Lys Tyr Thr Ala Asp             340 345 350 Asp Gly Thr Ser Lys Thr Ala Leu Asn Lys Leu Gly Gly Ala Asp Gly         355 360 365 Lys Thr Glu Val Val Ser Ile Gly Gly Lys Thr Tyr Ala Ala Ser Lys     370 375 380 Ala Glu Gly His Asn Phe Lys Ala Gln Pro Asp Leu Ala Glu Ala Ala 385 390 395 400 Ala Thr Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala                 405 410 415 Gln Val Asp Thr Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe             420 425 430 Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Thr Ser         435 440 445 Val Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn     450 455 460 Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala 465 470 475 480 Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 485 490 <210> 2 <211> 506 <212> PRT <213> Salmonella typhimurium <400> 2 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met 305 310 315 320 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu                 325 330 335 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly             340 345 350 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr         355 360 365 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val     370 375 380 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His 385 390 395 400 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr                 405 410 415 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala             420 425 430 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile         435 440 445 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg     450 455 460 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala 465 470 475 480 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln                 485 490 495 Val Pro Gln Asn Val Leu Ser Leu Leu Arg             500 505 <210> 3 <211> 492 <212> PRT <213> Escherichia coli <400> 3 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ser Leu Ser Ser Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Val Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Ile Arg Glu Leu Ser                 85 90 95 Val Gln Ala Thr Asn Gly Thr Asn Ser Asp Ser Asp Leu Ser Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Glu Glu Ile Asp Arg Val Ser Glu         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Glu Asn Asn Glu Met     130 135 140 Lys Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Thr Ile Asn Leu 145 150 155 160 Ala Lys Ile Asp Ala Lys Thr Leu Gly Leu Asp Gly Phe Asn Ile Asp                 165 170 175 Gly Ala Gln Lys Ala Thr Gly Ser Asp Leu Ile Ser Lys Phe Lys Ala             180 185 190 Thr Gly Thr Asp Asn Tyr Asp Val Gly Gly Lys Thr Tyr Thr Val Asn         195 200 205 Val Glu Ser Gly Ala Val Lys Asn Asp Ala Asn Lys Asp Val Phe Val     210 215 220 Ser Ala Asp Gly Ser Leu Thr Thr Ser Ser Asp Thr Lys Val Ser 225 230 235 240 Gly Glu Ser Ile Asp Ala Thr Glu Leu Ala Lys Leu Ala Ile Lys Leu                 245 250 255 Ala Asp Lys Gly Ser Ile Glu Tyr Lys Gly Ile Thr Phe Thr Asn Asn             260 265 270 Thr Gly Ala Glu Leu Asp Ala Asn Gly Lys Gly Val Leu Thr Ala Asn         275 280 285 Ile Asp Gly Gln Asp Val Gln Phe Thr Ile Asp Ser Asn Ala Pro Thr     290 295 300 Gly Ala Gly Ala Thr Ile Thr Thr Asp Thr Ala Val Tyr Lys Asn Ser 305 310 315 320 Ala Gly Gln Phe Thr Thr Thr Lys Val Glu Asn Lys Ala Ala Thr Leu                 325 330 335 Ser Asp Leu Asp Leu Asn Ala Ala Lys Lys Thr Gly Ser Thr Leu Val             340 345 350 Val Asn Gly Ala Thr Tyr Asn Val Ser Ala Asp Gly Lys Thr Val Thr         355 360 365 Asp Thr Thr Pro Gly Ala Pro Lys Val Met Tyr Leu Ser Lys Ser Glu     370 375 380 Gly Gly Ser Pro Ile Leu Val Asn Glu Asp Ala Ala Lys Ser Leu Gln 385 390 395 400 Ser Thr Thr Asn Pro Leu Glu Thr Ile Asp Lys Ala Leu Ala Lys Val                 405 410 415 Asp Asn Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asp Ser             420 425 430 Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Ser Ala Arg         435 440 445 Ser Arg Ile Glu Asp Ala Asp Tyr Ala Thr Glu Val Ser Asn Met Ser     450 455 460 Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala 465 470 475 480 Asn Gln Thr Thr Gln Asn Val Leu Ser Leu Leu Arg                 485 490 <210> 4 <211> 488 <212> PRT <213> Pseudomonas aeruginosa <400> 4 Met Ala Leu Thr Val Asn Thr Asn Ile Ala Ser Leu Asn Thr Gln Arg  1 5 10 15 Asn Leu Asn Ala Ser Ser Asn Asp Leu Asn Thr Ser Leu Gln Arg Leu             20 25 30 Thr Thr Gly Tyr Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Leu         35 40 45 Gln Ile Ser Asn Arg Leu Ser Asn Gln Ile Ser Gly Leu Asn Val Ala     50 55 60 Thr Arg Asn Ala Asn Asp Gly Ile Ser Leu Ala Gln Thr Ala Glu Gly 65 70 75 80 Ala Leu Gln Gln Ser Thr Asn Ile Leu Gln Arg Ile Arg Asp Leu Ala                 85 90 95 Leu Gln Ser Ala Asn Gly Ser Asn Ser Asp Ala Asp Arg Ala Ala Leu             100 105 110 Gln Lys Glu Val Ala Gln Gln Ala Glu Leu Thr Arg Ile Ser Asp         115 120 125 Thr Thr Thr Ply Gly Gly Arg Lys Leu Leu Asp Gly Ser Phe Gly Thr     130 135 140 Thr Ser Phe Gln Val Gly Ser Asn Ala Tyr Glu Thr Ile Asp Ile Ser 145 150 155 160 Leu Gln Asn Ala Ser Ala Ser Ala Ile Gly Ser Tyr Gln Val Gly Ser                 165 170 175 Asn Gly Ala Gly Thr Val Ala Ser Val Ala Gly Thr Ala Thr Ala Ser             180 185 190 Gly Ile Ala Ser Gly Thr Val Asn Leu Val Gly Gly Gly Gln Val Lys         195 200 205 Asn Ile Ala Ala Ala Gly Asp Ser Ala Lys Ala Ile Ala Glu Lys     210 215 220 Met Asp Gly Ala Ile Pro Asn Leu Ser Ala Arg Ala Arg Thr Val Phe 225 230 235 240 Thr Ala Asp Val Ser Gly Val Thr Gly Gly Ser Leu Asn Phe Asp Val                 245 250 255 Thr Val Gly Ser Asn Thr Val Ser Leu Ala Gly Val Thr Ser Thr Gln             260 265 270 Asp Leu Ala Asp Gln Leu Asn Ser Asn Ser Ser Lys Leu Gly Ile Thr         275 280 285 Ala Ser Ile Asn Asp Lys Gly Val Leu Thr Ile Thr Ser Ala Thr Gly     290 295 300 Glu Asn Val Lys Phe Gly Ala Gln Thr Gly Thr Ala Thr Ala Gly Gln 305 310 315 320 Val Ala Val Lys Val Gln Gly Ser Asp Gly Lys Phe Glu Ala Ala Ala                 325 330 335 Lys Asn Val Ala Ala Gly Thr Ala Ala Thr Thr Thr Ile Val Thr             340 345 350 Gly Tyr Val Gln Leu Asn Ser Pro Thr Ala Tyr Ser Val Ser Gly Thr         355 360 365 Gly Thr Gln Ala Ser Gln Val Phe Gly Asn Ala Ser Ala Ala Gln Lys     370 375 380 Ser Ser Val Ala Ser Val Asp Ile Ser Thr Ala Asp Gly Ala Gln Asn 385 390 395 400 Ala Ile Ala Val Val Asp Asn Ala Leu Ala Ala Ile Asp Ala Gln Arg                 405 410 415 Ala Asp Leu Gly Ala Val Gln Asn Arg Phe Lys Asn Thr Ile Asp Asn             420 425 430 Leu Thr Asn Ile Ser Glu Asn Ala Thr Asn Ala Arg Ser Ser Ile Lys         435 440 445 Asp Thr Asp Phe Ala Ala Glu Thr Ala Ala Leu Ser Lys Asn Gln Val     450 455 460 Leu Gln Gln Ala Gly Thr Ala Ile Leu Ala Gln Ala Asn Gln Leu Pro 465 470 475 480 Gln Ala Val Leu Ser Leu Leu Arg                 485 <210> 5 <211> 518 <212> PRT <213> Aquifex aeolicus <400> 5 Met Ala Thr Arg Ile Asn Tyr Asn Tyr Glu Ala Ala Val Thr Tyr Thr  1 5 10 15 Ser Leu Lys Gln Asn Glu Arg Leu Met Asn Lys Ser Leu Leu Arg Leu             20 25 30 Ser Thr Gly Leu Arg Ile Leu Ser Ala Ala Asp Asp Ala Ser Gly Leu         35 40 45 Phe Ile Ala Asp Gln Leu Ala Leu Val Ser Ala Gly Leu Glu Gln Gly     50 55 60 Asn Arg Asn Ile Gln Phe Gly Ile Ser Ala Leu Gln Ile Ala Glu Gly 65 70 75 80 Gly Val Ser Gln Ile Tyr Asp Lys Leu Lys Thr Met Tyr Gln Lys Ala                 85 90 95 Val Ser Ala Aslan Asp Aslan Asp As Aslan Pro Asn Ala Arg Ala Ala Leu             100 105 110 Gln Arg Asp Ile Glu Asn Leu Arg Asp Ala Ile Leu Lys Ile Ala Gln         115 120 125 Asp Thr Glu Tyr Asn Gly Ile Arg Leu Leu Asn Gly Ser Phe Asn Asn     130 135 140 Val Arg Ile His Tyr Gly Ala Arg Ser Ala Gln Thr Leu Ser Val Ser 145 150 155 160 Ile Ser Ser Val Leu Pro Gln Gln Leu Gly Gly Tyr Val Ala Glu Asp                 165 170 175 Ser Pro Ala Thr Ala Thr Asp Thr Asn Asn Val Leu Thr Asn Ile Gly             180 185 190 Thr Asn Thr Asn Tyr Ser Val Ala Ser Gly Asp Ser Leu Ala Phe         195 200 205 Thr Phe Thr Asp Gly Thr Ser Ile Thr Phe Asn Ser Leu Asn Gln Leu     210 215 220 Gly Tyr Asp Phe Asn Asn Thr Gly Thr Tyr Ile Leu Asp Ala Ser Ala 225 230 235 240 Ile Val Asn Thr Ile Asn Asn Asn Pro Thr Leu Gln Gly Lys Gly Ile                 245 250 255 Arg Ala Tyr Ala Glu Asn Val Ser Glu Ala Asp Leu Thr Phe Asp Thr             260 265 270 Thr Asn Val Asn Ile Asp Gln Gly Asp Glu Val Thr Ile Thr Phe Tyr         275 280 285 Ser Gly Gly Glu Leu Val Phe Thr Lys Thr Tyr Thr Asp Thr Val Thr     290 295 300 Leu Asp Gln Phe Ile Ala Asp Ile Asn Asn Gln Ala Gly Gly Lys Leu 305 310 315 320 Ile Ala Ser Lys Asp Pro Ser Gly Thr Lys Leu Val Leu Ser Thr Pro                 325 330 335 Asn Gly Glu Thr Ile Ser Val Glu Val Thr Val Asn Asp Ala Asp Gly             340 345 350 Asp Thr Val Ser Ser Ile Asn Leu Gly Ala Leu Leu Gln Gly Ala         355 360 365 Ala Gly Thr Val Val Asn Thr Ser Gly Ala Thr Ala Ser Ala Val Lys     370 375 380 Val Gly Thr Leu Ile Val Met Gly Ser Glu Asn Phe Thr Val Gln Gly 385 390 395 400 Thr Gly Ile Ala Tyr Phe Thr Ala Ala Thr Ser Gly Thr Phe Asn Ser                 405 410 415 Leu Asn Asp Val Asp Val Thr Thr Asn Lys Gly Ala Glu Ile Ala Gln             420 425 430 Val Leu Ile Gln Arg Ala Val Arg Gln Val Asp Thr Ile Arg Thr Gln         435 440 445 Ile Gly Ser Thr Ile Asn Asn Leu Gln Ala Ile Tyr Asp Ala Gln Ala     450 455 460 Val Ala Lys Asp Asn Thr Asp Asn Ala Glu Ser Ile Ile Arg Asn Val 465 470 475 480 Asp Phe Ala Lys Glu Met Thr Glu Phe Thr Lys Tyr Gln Ile Arg Met                 485 490 495 Gln Ser Gly Val Ala Met Leu Ala Gln Ala Asn Ala Leu Pro Gln Leu             500 505 510 Val Leu Gln Leu Leu Arg         515 <210> 6 <211> 510 <212> PRT <213> Helicobacter pylori <400> 6 Met Ala Phe Gln Val Asn Thr Asn Ile Asn Ala Met Asn Ala His Val  1 5 10 15 Gln Ser Ala Leu Thr Gln Asn Ala Leu Lys Thr Ser Leu Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Lys Ala Ala Asp Asp Ala Ser Gly Met         35 40 45 Thr Val Ala Asp Ser Leu Arg Ser Gln Ala Ser Ser Leu Gly Gln Ala     50 55 60 Ile Ala Asn Thr Asn Asp Gly Met Gly Ile Ile Gln Val Ala Asp Lys 65 70 75 80 Ala Met Asp Glu Gln Leu Lys Ile Leu Asp Thr Val Lys Val Lys Ala                 85 90 95 Thr Gln Ala Ala Gln Asp Gly Gln Thr Thr Glu Ser Arg Lys Ala Ile             100 105 110 Gln Ser Asp Ile Val Arg Leu Ile Gln Gly Leu Asp Asn Ile Gly Asn         115 120 125 Thr Thr Thr Asn Gly Gln Ala Leu Leu Ser Gly Gln Phe Thr Asn     130 135 140 Lys Glu Phe Gln Val Gly Ala Tyr Ser Asn Gln Ser Ile Lys Ala Ser 145 150 155 160 Ile Gly Ser Thr Thr Ser Asp Lys Ile Gly Gln Val Arg Ile Ala Thr                 165 170 175 Gly Ala Leu Ile Thr Ala Ser Gly Asp Ile Ser Leu Thr Phe Lys Gln             180 185 190 Val Asp Gly Val Asn Asp Val Thr Leu Glu Ser Val Lys Val Ser Ser         195 200 205 Ser Ala Gly Thr Gly Ile Gly Val Leu Ala Glu Val Ile Asn Lys Asn     210 215 220 Ser Asn Arg Thr Gly Val Lys Ala Tyr Ala Ser Val Ile Thr Thr Ser 225 230 235 240 Asp Val Ala Val Gln Ser Gly Ser Leu Ser Asn Leu Thr Leu Asn Gly                 245 250 255 Ile His Leu Gly Asn Ile Ala Asp Ile Lys Lys Asn Asp Ser Asp Gly             260 265 270 Arg Leu Val Ala Ile Asn Ala Val Thr Ser Glu Thr Gly Val Glu         275 280 285 Ala Tyr Thr Asp Gln Lys Gly Arg Leu Asn Leu Arg Ser Ile Asp Gly     290 295 300 Arg Gly Ile Glu Ile Lys Thr Asp Ser Val Ser Asn Gly Ser Ser Ala 305 310 315 320 Leu Thr Met Val Asn Gly Gly Gln Asp Leu Thr Lys Gly Ser Thr Asn                 325 330 335 Tyr Gly Arg Leu Ser Leu Thr Arg Leu Asp Ala Lys Ser Ile Asn Val             340 345 350 Val Ser Ala Ser Asp Ser Gln His Leu Gly Phe Thr Ala Ile Gly Phe         355 360 365 Gly Glu Ser Gln Val Ala Glu Thr Thr Val Asn Leu Arg Asp Val Thr     370 375 380 Gly Asn Phe Asn Ala Asn Val Lys Ser Ala Ser Gly Ala Asn Tyr Asn 385 390 395 400 Ala Val Ile Ala Ser Gly Asn Gln Ser Leu Gly Ser Gly Val Thr Thr                 405 410 415 Leu Arg Gly Ala Met Val Val Ile Asp Ile Ala Glu Ser Ala Met Lys             420 425 430 Met Leu Asp Lys Val Arg Ser Asp Leu Gly Ser Val Gln Asn Gln Met         435 440 445 Ile Ser Thr Val Asn Asn Ile Ser Ile Thr Gln Val Asn Val Lys Ala     450 455 460 Ala Glu Ser Gln Ile Arg Asp Val Asp Phe Ala Glu Glu Ser Ala Asn 465 470 475 480 Phe Asn Lys Asn Asn Ile Leu Ala Gln Ser Gly Ser Tyr Ala Met Ser                 485 490 495 Gln Ala Asn Thr Val Gln Gln Asn Ile Leu Arg Leu Leu Thr             500 505 510 <210> 7 <211> 475 <212> PRT <213> Legionella pneumophila <400> 7 Met Ala Gln Val Ile Asn Thr Asn Val Ala Ser Leu Thr Ala Gln Arg  1 5 10 15 Asn Leu Gly Val Ser Gly Asn Met Met Gln Thr Ser Ile Gln Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Leu         35 40 45 Ala Ile Ser Gln Arg Met Thr Ala Gln Ile Arg Gly Met Asn Gln Ala     50 55 60 Val Arg Asn Ala Asn Asp Gly Ile Ser Leu Ser Gln Val Ala Glu Gly 65 70 75 80 Ala Met Gln Glu Thr Thr Asn Ile Leu Gln Arg Met Met Glu Leu Ser                 85 90 95 Val Gln Ala Ala Asn Ser Thr Asn Asn Ser Ser Asp Arg Ala Ser Ile             100 105 110 Gln Ser Glu Ile Ser Gln Leu Lys Ser Glu Leu Glu Arg Ile Ala Gln         115 120 125 Asn Thr Glu Phe Asn Gly Gln Arg Ile Leu Asp Gly Ser Phe Ser Gly     130 135 140 Ala Ser Phe Gln Val Gly Ala Asn Ser Asn Gln Thr Ile Asn Phe Ser 145 150 155 160 Ile Gly Ser Ile Lys Ala Ser Ile Gly Ily Ale Thr Ala Thr                 165 170 175 Gly Thr Glu Val Ala Gly Ala Ala Ala Thr Asp Ile Thr Ile Ala Ile             180 185 190 Gly Gly Gly Ala Ala Thr Ser Ile Asn Ser Ser Ala Asn Phe Thr Gly         195 200 205 Ala Leu Asn Gly Gln Asp Ala Thr Ser Ala Tyr Ala Lys Ala Ala Ala     210 215 220 Ile Asn Asp Ala Gly Ile Gly Gly Leu Ser Val Thr Ala Ser Thr Ser 225 230 235 240 Gly Thr Gln Ala Gly Asp Thr Tyr                 245 250 255 Asn Leu Thr Asle Asn Gly Aslan Ile Tyr Aslan Leu Asp Val Ala             260 265 270 Thr Ala Leu Thr Asn Ser Asp Leu Arg Asp Ala Ile Asn Gly Val Ser         275 280 285 Asn Gln Thr Gly Val Val Ala Ser Leu Asn Gly Gly Asn Met Thr Leu     290 295 300 Thr Ala Asp Gly Arg Asn Ile Thr Val Thr Glu Ser Gly Thr Gly 305 310 315 320 Phe Thr Ala Gly Thr Asp Gly Leu Thr Val Thr Gly Gly Ala Phe Asp                 325 330 335 Gly Arg Leu Arg Gly Thr Leu Ser Ile Ser Ala Val Asp Thr Ile Ala             340 345 350 Ile Gly Gly Thr Val Ala Asn Ile Gly Leu Ser Ala Asn Ile Ser Lys         355 360 365 Asp Thr Val Gly Ile Asp Ser Leu Asp Val Ser Thr Gly Ser Gly Arg     370 375 380 Gln Thr Ala Ile Lys Arg Ile Asp Ala Ala Leu Asn Ser Val Asn Ser 385 390 395 400 Asn Arg Ala Asn Met Gly Ala Leu Gln Asn Arg Phe Glu Ser Thr Ile                 405 410 415 Ala Asn Leu Glu Asn Val Ser Asp Asn Leu Ser Ala Ala Arg Ser Arg             420 425 430 Ile Gln Asp Ala Asp Tyr Ala Ala Glu Met Ala Ser Leu Thr Lys Asn         435 440 445 Gln Ile Leu Gln Gln Ala Gly Thr Ala Met Leu Ala Gln Ala Asn Ser     450 455 460 Leu Pro Gln Ser Val Leu Ser Leu Leu Gly Arg 465 470 475 <210> 8 <211> 293 <212> PRT <213> Artificial Sequence <220> <223> B / Florida / 4/2006 HA 1-1 <400> 8 Thr Thr Pro Thr Lys Ser Tyr Phe Ala Asn Leu Lys Gly Thr Arg  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys         35 40 45 Ala Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu                 85 90 95 Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val     130 135 140 Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe 145 150 155 160 His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser Asn                 165 170 175 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val             180 185 190 Ser Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro         195 200 205 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys     210 215 220 Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val 225 230 235 240 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu                 245 250 255 Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys             260 265 270 Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys         275 280 285 Pro Ile Trp Val Lys     290 <210> 9 <211> 294 <212> PRT <213> Artificial Sequence <220> <223> B / Malaysia / 2506/2004 HA 1-1 <400> 9 Thr Thr Thr Pro Thr Lys Ser His Phe Ala Asn Leu Lys Gly Thr Glu  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Asn Ile Pro Ser Ala Arg         35 40 45 Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn Ala Glu                 85 90 95 Asn Ala Pro Gly Gly Ser Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asn Asp Asn Asn Lys Thr Ala Thr Asn Ser Leu Thr Ile Glu     130 135 140 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly 145 150 155 160 Phe His Ser Asp Asn Glu Ala Gln Met Ala Lys Leu Tyr Gly Asp Ser                 165 170 175 Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr             180 185 190 Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu         195 200 205 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly     210 215 220 Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys 225 230 235 240 Val Trp Cys Ala Ser Gly Arg Ser Ser Lys Val Ile Lys Gly Ser Leu Pro                 245 250 255 Leu Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn             260 265 270 Lys Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn         275 280 285 Cys Pro Ile Trp Val Lys     290 <210> 10 <211> 272 <212> PRT <213> Artificial Sequence <220> <223> A / Solomon Islands / 3/2006 HA1-1 <400> 10 Ser His Asn Gly Lys Leu Cys Leu Leu Lys Gly Ile Ala Pro Leu Gln  1 5 10 15 Leu Gly Asn Cys Ser Val Ala Gly Trp Ile Leu Gly Asn Pro Glu Cys             20 25 30 Glu Leu Leu Ile Ser Arg Glu Ser Trp Ser Tyr Ile Val Glu Lys Pro         35 40 45 Asn Pro Glu Asn Gly Thr Cys Tyr Pro Gly His Phe Ala Asp Tyr Glu     50 55 60 Glu Leu Arg Glu Gln Leu Ser Ser Val Ser Ser Phe Glu Arg Phe Glu 65 70 75 80 Ile Phe Pro Lys Glu Ser Ser Trp Pro Asn His Thr Thr Thr Gly Val                 85 90 95 Ser Ala Ser Cys Ser His Asn Gly Glu Ser Ser Phe Tyr Lys Asn Leu             100 105 110 Leu Trp Leu Thr Gly Lys Asn Gly Leu Tyr Pro Asn Leu Ser Lys Ser         115 120 125 Tyr Ala Asn Asn Lys Glu Lys Glu Val Leu Val Leu Trp Gly Val His     130 135 140 His Pro Pro Asn Ile Gly Asp Gln Arg Ala Leu Tyr His Lys Glu Asn 145 150 155 160 Ala Tyr Val Ser Val Val Ser Ser His Tyr Ser Arg Lys Phe Thr Pro                 165 170 175 Glu Ile Ala Lys Arg Pro Lys Val Arg Asp Gln Glu Gly Arg Ile Asn             180 185 190 Tyr Tyr Trp Thr Leu Leu Glu Pro Gly Asp Thr Ile Ile Phe Glu Ala         195 200 205 Asn Gly Asn Leu Ile Ala Pro Arg Tyr Ala Phe Ala Leu Ser Arg Gly     210 215 220 Phe Gly Ser Gly Ile Ile Asn Ser Asn Ala Pro Met Asp Glu Cys Asp 225 230 235 240 Ala Lys Cys Gln Thr Pro Gln Gly Ala Ile Asn Ser Ser Leu Pro Phe                 245 250 255 Gln Asn Val His Pro Val Thr Ile Gly Glu Cys Pro Lys Tyr Val Arg             260 265 270 <210> 11 <211> 267 <212> PRT <213> Artificial Sequence <220> <223> A / Perth / 16/2009 HA1-1 <400> 11 Gln Ser Ser Ser Thr Gly Glu Ile Cys Asp Ser Pro His Gln Ile Leu  1 5 10 15 Asp Gly Lys Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln             20 25 30 Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val Glu Arg Ser         35 40 45 Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser     50 55 60 Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe Asn Asn Glu 65 70 75 80 Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser Ser Ala Cys                 85 90 95 Ile Arg Arg Ser Lys Asn Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr             100 105 110 His Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr Met Pro Asn Asn         115 120 125 Glu Gln Phe Asp Lys Leu Tyr Ile Trp Gly Val His His Pro Gly Thr     130 135 140 Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ala Ser Gly Arg Ile Thr 145 150 155 160 Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ser Pro Asn Ile Gly Ser                 165 170 175 Arg Pro Arg Val Arg Asn Ile Pro Ser Arg Ile Ser Ile Tyr Trp Thr             180 185 190 Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu         195 200 205 Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile     210 215 220 Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu Cys Ile Thr 225 230 235 240 Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn Val Asn Arg                 245 250 255 Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys             260 265 <210> 12 <211> 267 <212> PRT <213> Artificial Sequence <220> <223> A / Wyoming / 03/2003 HA1-1 <400> 12 Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro His Gln Ile Leu  1 5 10 15 Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln             20 25 30 Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val Glu Arg Ser         35 40 45 Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser     50 55 60 Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe Asn Asn Glu 65 70 75 80 Ser Phe Asn Trp Ala Gly Val Thr Gln Asn Gly Thr Ser Ser Ala Cys                 85 90 95 Lys Arg Arg Ser Asn Lys Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr             100 105 110 His Leu Lys Tyr Lys Tyr Pro Ala Leu Asn Val Thr Met Pro Asn Asn         115 120 125 Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly Val His His Pro Val Thr     130 135 140 Asp Ser Asp Gln Ile Ser Leu Tyr Ala Gln Ala Ser Gly Arg Ile Thr 145 150 155 160 Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn Ile Gly Tyr                 165 170 175 Arg Pro Arg Val As Asp Ile Ser Ser Arg Ile Ser Ile Tyr Trp Thr             180 185 190 Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu         195 200 205 Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile     210 215 220 Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu Cys Ile Thr 225 230 235 240 Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn Val Asn Arg                 245 250 255 Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys             260 265 <210> 13 <211> 267 <212> PRT <213> Artificial Sequence <220> <223> A / New York / 2782/2004 <400> 13 Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro His Gln Ile Leu  1 5 10 15 Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln             20 25 30 Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val Glu Arg Ser         35 40 45 Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser     50 55 60 Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe Asn Asn Glu 65 70 75 80 Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser Ser Ala Cys                 85 90 95 Lys Arg Arg Ser Asn Ser Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr             100 105 110 His Leu Lys Phe Lys Tyr Pro Ala Leu Asn Val Thr Met Pro Asn Asn         115 120 125 Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly Val His His Pro Ser Thr     130 135 140 Asp Asn Gln Ile Ser Leu Tyr Ala Gln Ala Ser Gly Arg Ile Thr 145 150 155 160 Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn Ile Gly Ser                 165 170 175 Arg Pro Arg Val As Asp Ile Pro Ser Arg Ile Ser Ile Tyr Trp Thr             180 185 190 Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu         195 200 205 Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile     210 215 220 Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu Cys Ile Thr 225 230 235 240 Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn Val Asn Arg                 245 250 255 Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys             260 265 <210> 14 <211> 267 <212> PRT <213> Artificial Sequence <220> <223> A / Victoria / 361/2011 HA1-1 <400> 14 Gln Asn Ser Ser Ile Gly Glu Ile Cys Asp Ser Pro His Gln Ile Leu  1 5 10 15 Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln             20 25 30 Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val Glu Arg Ser         35 40 45 Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser     50 55 60 Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe Asn Asn Glu 65 70 75 80 Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser Ser Ala Cys                 85 90 95 Ile Arg Arg Ser Asn Asn Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr             100 105 110 Gln Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr Met Pro Asn Asn         115 120 125 Glu Gln Phe Asp Lys Leu Tyr Ile Trp Gly Val His His Pro Val Thr     130 135 140 Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ser Ser Gly Arg Ile Thr 145 150 155 160 Val Ser Thr Lys Arg Ser Gln Gln Ala Val Ile Pro Asn Ile Gly Tyr                 165 170 175 Arg Pro Arg Ile Arg Asn Ile Pro Ser Arg Ile Ser Ile Tyr Trp Thr             180 185 190 Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu         195 200 205 Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile     210 215 220 Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu Cys Ile Thr 225 230 235 240 Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn Val Asn Arg                 245 250 255 Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys             260 265 <210> 15 <211> 267 <212> PRT <213> Artificial Sequence <220> <223> A / Aichi / 2/68 HA1-1 <400> 15 Gln Ser Ser Thr Gly Lys Ile Cys Asn Asn Pro His Arg Ile Leu  1 5 10 15 Asp Gly Ile Asp Cys Thr Leu Ile Asp Ala Leu Leu Gly Asp Pro His             20 25 30 Cys Asp Val Phe Gln Asn Glu Thr Trp Asp Leu Phe Val Glu Arg Ser         35 40 45 Lys Ala Phe Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser     50 55 60 Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe Ile Thr Glu 65 70 75 80 Gly Phe Thr Trp Thr Gly Val Thr Gln Asn Gly Gly Ser Asn Ala Cys                 85 90 95 Lys Arg Gly Pro Gly Ser Gly Phe Phe Ser Arg Leu Asn Trp Leu Thr             100 105 110 Lys Ser Gly Ser Thr Tyr Pro Val Leu Asn Val Thr Met Pro Asn Asn         115 120 125 Asp Asn Phe Asp Lys Leu Tyr Ile Trp Gly Ile His His Pro Ser Thr     130 135 140 Asn Gln Glu Gln Thr Ser Leu Tyr Val Gln Ala Ser Gly Arg Val Thr 145 150 155 160 Val Ser Thr Arg Arg Ser Gln Gln Thr Ile Ile Pro Asn Ile Gly Ser                 165 170 175 Arg Pro Trp Val Arg Gly Leu Ser Ser Arg Ile Ser Ile Tyr Trp Thr             180 185 190 Ile Val Lys Pro Gly Asp Val Leu Val Ile Asn Ser Asn Gly Asn Leu         195 200 205 Ile Ala Pro Arg Gly Tyr Phe Lys Met Arg Thr Gly Lys Ser Ser Ile     210 215 220 Met Arg Ser Asp Ala Pro Ile Asp Thr Cys Ile Ser Glu Cys Ile Thr 225 230 235 240 Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn Val Asn Lys                 245 250 255 Ile Thr Tyr Gly Ala Cys Pro Lys Tyr Val Lys             260 265 <210> 16 <211> 267 <212> PRT <213> Artificial Sequence <220> <223> A / Wisconsin / 67/2005 HA1-1 <400> 16 Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro His Gln Ile Leu  1 5 10 15 Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln             20 25 30 Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val Glu Arg Ser         35 40 45 Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser     50 55 60 Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe Asn Asp Glu 65 70 75 80 Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser Ser Ala Cys                 85 90 95 Lys Arg Arg Ser Asn Asn Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr             100 105 110 His Leu Lys Phe Lys Tyr Pro Ala Leu Asn Val Thr Met Pro Asn Asn         115 120 125 Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly Val His His Pro Gly Thr     130 135 140 Asp Asn Gln Ile Phe Leu His Ala Gln Ala Ser Gly Arg Ile Thr 145 150 155 160 Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn Ile Gly Ser                 165 170 175 Arg Pro Arg Ile Arg Asn Ile Pro Ser Arg Ile Ser Ile Tyr Trp Thr             180 185 190 Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu         195 200 205 Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile     210 215 220 Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu Cys Ile Thr 225 230 235 240 Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn Val Asn Arg                 245 250 255 Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys             260 265 <210> 17 <211> 274 <212> PRT <213> Artificial Sequence <220> <223> A / Anhui / 1/2005 HA1-1 <400> 17 Glu Lys Thr His Asn Gly Lys Leu Cys Asp Leu Asp Gly Val Lys Pro  1 5 10 15 Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu Leu Gly Asn Pro             20 25 30 Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser Tyr Ile Val Glu         35 40 45 Lys Ala Asn Pro Ala Asn Asp Leu Cys Tyr Pro Gly Asn Phe Asn Asp     50 55 60 Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn His Phe Glu Lys 65 70 75 80 Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His Glu Ala Ser Ser                 85 90 95 Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly Thr Pro Ser Phe Phe Arg             100 105 110 Asn Val Val Trp Leu Ile Lys Lys Asn Asn Thr Tyr Pro Thr Ile Lys         115 120 125 Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu Ile Leu Trp Gly     130 135 140 Ile His His Ser Asn Asp Ala Ala Glu Gln Thr Lys Leu Tyr Gln Asn 145 150 155 160 Pro Thr Thr Ile Ser Val Gly Thr Ser Thr Leu Asn Gln Arg Leu                 165 170 175 Val Pro Lys Ile Ala Thr Arg Ser Lys Val Asn Gly Gln Ser Gly Arg             180 185 190 Met Asp Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp Ala Ile Asn Phe         195 200 205 Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val     210 215 220 Lys Lys Gly Asp Ser Ala Ile Val Lys Ser Glu Val Glu Tyr Gly Asn 225 230 235 240 Cys Asn Thr Lys Cys Gln Thr Pro Ile Gly Ala Ile Asn Ser Ser Met                 245 250 255 Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr             260 265 270 Val Lys          <210> 18 <211> 274 <212> PRT <213> Artificial Sequence <220> <223> A / Bar headed goose / Qinghai / 1A / 2005 HA1-1 <400> 18 Glu Lys Thr His Asn Gly Lys Leu Cys Asp Leu Asp Gly Val Lys Pro  1 5 10 15 Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu Leu Gly Asn Pro             20 25 30 Met Cys Asp Glu Phe Leu Asn Val Pro Glu Trp Ser Tyr Ile Val Glu         35 40 45 Lys Ile Asn Pro Ala Asn Asp Leu Cys Tyr Pro Gly Asn Phe Asn Asp     50 55 60 Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn His Phe Glu Lys 65 70 75 80 Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His Glu Ala Ser Ser                 85 90 95 Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly Arg Ser Ser Phe Phe Arg             100 105 110 Asn Val Val Trp Leu Ile Lys Lys Asn Asn Ala Tyr Pro Thr Ile Lys         115 120 125 Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu Val Leu Trp Gly     130 135 140 Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Arg Leu Tyr Gln Asn 145 150 155 160 Pro Thr Thr Ile Ser Val Gly Thr Ser Thr Leu Asn Gln Arg Leu                 165 170 175 Val Pro Lys Ile Ala Thr Arg Ser Lys Val Asn Gly Gln Ser Gly Arg             180 185 190 Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp Ala Ile Asn Phe         195 200 205 Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Asn Ala Tyr Lys Ile Val     210 215 220 Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu Leu Glu Tyr Gly Asn 225 230 235 240 Cys Asn Thr Lys Cys Gln Thr Pro Ile Gly Ala Ile Asn Ser Ser Met                 245 250 255 Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr             260 265 270 Val Lys          <210> 19 <211> 274 <212> PRT <213> Artificial Sequence <220> <223> A / Indonesia / 5/2005 HA1-1 <400> 19 Glu Lys Thr His Asn Gly Lys Leu Cys Asp Leu Asp Gly Val Lys Pro  1 5 10 15 Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu Leu Gly Asn Pro             20 25 30 Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser Tyr Ile Val Glu         35 40 45 Lys Ala Asn Pro Thr Asn Asp Leu Cys Tyr Pro Gly Ser Phe Asn Asp     50 55 60 Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn His Phe Glu Lys 65 70 75 80 Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His Glu Ala Ser Ser                 85 90 95 Gly Val Ser Ser Ala Cys Pro Tyr Leu Gly Ser Ser Ser Phe Phe Arg             100 105 110 Asn Val Val Trp Leu Ile Lys Lys Asn Ser Thr Tyr Pro Thr Ile Lys         115 120 125 Lys Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu Val Leu Trp Gly     130 135 140 Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Arg Leu Tyr Gln Asn 145 150 155 160 Pro Thr Thr Ile Ser Ile Gly Thr Ser Thr Leu Asn Gln Arg Leu                 165 170 175 Val Pro Lys Ile Ala Thr Arg Ser Lys Val Asn Gly Gln Ser Gly Arg             180 185 190 Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp Ala Ile Asn Phe         195 200 205 Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val     210 215 220 Lys Lys Gly Asp Ser Ala Ile Met Lys Ser Glu Leu Glu Tyr Gly Asn 225 230 235 240 Cys Asn Thr Lys Cys Gln Thr Pro Met Gly Ala Ile Asn Ser Ser Met                 245 250 255 Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr             260 265 270 Val Lys          <210> 20 <211> 274 <212> PRT <213> Artificial Sequence <220> <223> A / Vietnam / 1203/2004 HA1-1 <400> 20 Glu Lys Lys His Asn Gly Lys Leu Cys Asp Leu Asp Gly Val Lys Pro  1 5 10 15 Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu Leu Gly Asn Pro             20 25 30 Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser Tyr Ile Val Glu         35 40 45 Lys Ala Asn Pro Val Asn Asp Leu Cys Tyr Pro Gly Asp Phe Asn Asp     50 55 60 Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn His Phe Glu Lys 65 70 75 80 Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Ser His Glu Ala Ser Leu                 85 90 95 Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly Lys Ser Ser Phe Phe Arg             100 105 110 Asn Val Val Trp Leu Ile Lys Lys Asn Ser Thr Tyr Pro Thr Ile Lys         115 120 125 Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu Val Leu Trp Gly     130 135 140 Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Lys Leu Tyr Gln Asn 145 150 155 160 Pro Thr Thr Ile Ser Val Gly Thr Ser Thr Leu Asn Gln Arg Leu                 165 170 175 Val Pro Arg Ile Ala Thr Arg Ser Lys Val Asn Gly Gln Ser Gly Arg             180 185 190 Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp Ala Ile Asn Phe         195 200 205 Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val     210 215 220 Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu Leu Glu Tyr Gly Asn 225 230 235 240 Cys Asn Thr Lys Cys Gln Thr Pro Met Gly Ala Ile Asn Ser Ser Met                 245 250 255 Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr             260 265 270 Val Lys          <210> 21 <211> 274 <212> PRT <213> Artificial Sequence <220> <223> A / Hubei / 1/2010 HA1-1 <400> 21 Glu Lys Thr His Asn Gly Lys Leu Cys Asp Leu Asn Gly Val Lys Pro  1 5 10 15 Leu Ile Leu Lys Asp Cys Ser Val Ala Gly Trp Leu Leu Gly Asn Pro             20 25 30 Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser Tyr Ile Val Glu         35 40 45 Lys Ala Asn Pro Ala Asn Asp Leu Cys Tyr Pro Gly Asn Phe Asn Asp     50 55 60 Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn His Phe Glu Lys 65 70 75 80 Ile Gln Ile Ile Pro Lys Asn Ser Trp Ser Asp His Glu Ala Ser Leu                 85 90 95 Gly Val Ser Ala Ala Cys Pro Tyr Gln Gly Lys Ser Ser Phe Phe Arg             100 105 110 Asn Val Val Trp Leu Ile Lys Lys Asp Asn Ala Tyr Pro Thr Ile Lys         115 120 125 Lys Gly Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu Val Leu Trp Gly     130 135 140 Ile His His Pro Asn Asp Glu Ala Glu Gln Thr Arg Leu Tyr Gln Asn 145 150 155 160 Pro Thr Thr Ile Ser Ile Gly Thr Ser Thr Leu Asn Gln Arg Leu                 165 170 175 Val Pro Lys Ile Ala Thr Arg Ser Lys Ile Asn Gly Gln Ser Gly Arg             180 185 190 Ile Asp Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp Ala Ile His Phe         195 200 205 Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val     210 215 220 Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu Val Glu Tyr Gly Asn 225 230 235 240 Cys Asn Thr Arg Cys Gln Thr Pro Ile Gly Ala Ile Asn Ser Ser Met                 245 250 255 Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr             260 265 270 Val Lys          <210> 22 <211> 274 <212> PRT <213> Artificial Sequence <220> <223> A / Hong Kong / 156/97 HA1-1 <400> 22 Glu Arg Thr His Asn Gly Lys Leu Cys Asp Leu Asn Gly Val Lys Pro  1 5 10 15 Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu Leu Gly Asn Pro             20 25 30 Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser Tyr Ile Val Glu         35 40 45 Lys Ala Ser Pro Ala Asn Asp Leu Cys Tyr Pro Gly Asn Phe Asn Asp     50 55 60 Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn His Phe Glu Lys 65 70 75 80 Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asn His Asp Ala Ser Ser                 85 90 95 Gly Val Ser Ser Ala Cys Pro Tyr Leu Gly Arg Ser Ser Phe Phe Arg             100 105 110 Asn Val Val Trp Leu Ile Lys Lys Asn Ser Ala Tyr Pro Thr Ile Lys         115 120 125 Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu Val Leu Trp Gly     130 135 140 Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Lys Leu Tyr Gln Asn 145 150 155 160 Pro Thr Thr Ile Ser Val Gly Thr Ser Thr Leu Asn Gln Arg Leu                 165 170 175 Val Pro Glu Ile Ala Thr Arg Pro Lys Val Asn Gly Gln Ser Gly Arg             180 185 190 Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp Ala Ile Asn Phe         195 200 205 Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val     210 215 220 Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu Leu Glu Tyr Gly Asn 225 230 235 240 Cys Asn Thr Lys Cys Gln Thr Pro Met Gly Ala Ile Asn Ser Ser Met                 245 250 255 Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr             260 265 270 Val Lys          <210> 23 <211> 271 <212> PRT <213> Artificial Sequence <220> <223> A / Anhui / 1/2013 HA1-1 <400> 23 Glu Thr Val Glu Arg Thr Asn Ile Pro Arg Ile Cys Ser Lys Gly Lys  1 5 10 15 Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Ile Thr Gly             20 25 30 Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp Leu Ile Ile         35 40 45 Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys Phe Val Asn     50 55 60 Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly Ile Asp Lys 65 70 75 80 Glu Ala Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala Thr                 85 90 95 Ser Ala Cys Arg Arg Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys Trp             100 105 110 Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met Thr Lys Ser         115 120 125 Tyr Lys Asn Thr Arg Lys Ser Pro Ala Leu Ile Val Trp Gly Ile His     130 135 140 His Ser Val Ser Thr Ala Glu Gln Thr Lys Leu Tyr Gly Ser Gly Asn 145 150 155 160 Lys Leu Val Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser Phe Val Pro                 165 170 175 Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Leu Ser Gly Arg Ile Asp             180 185 190 Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr Val Thr Phe Ser Phe         195 200 205 Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu Arg Gly Lys     210 215 220 Ser Met Gly Ile Gln Ser Gly Val Gln Val Asp Ala Asn Cys Glu Gly 225 230 235 240 Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn Leu Pro Phe Gln                 245 250 255 Asn Ile Asp Ser Arg Ala Val Gly Lys Cys Pro Arg Tyr Val Lys             260 265 270 <210> 24 <211> 271 <212> PRT <213> Artificial Sequence <220> <223> A / Turkey / Italy / 214845/2002 HA1-1 <400> 24 Glu Thr Val Glu Arg Thr Asn Val Pro Arg Ile Cys Ser Lys Gly Lys  1 5 10 15 Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Ile Thr Gly             20 25 30 Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp Leu Ile Ile         35 40 45 Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys Phe Val Asn     50 55 60 Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly Ile Asp Lys 65 70 75 80 Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala Thr                 85 90 95 Ser Ala Cys Arg Arg Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys Trp             100 105 110 Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met Thr Lys Ser         115 120 125 Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile Trp Gly Ile His     130 135 140 His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr Gly Ser Gly Asn 145 150 155 160 Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser Phe Val Pro                 165 170 175 Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly Arg Ile Asp             180 185 190 Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr Val Thr Phe Ser Phe         195 200 205 Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu Arg Gly Lys     210 215 220 Ser Met Gly Ile Gln Ser Ser Val Gln Val Asp Ala Asn Cys Glu Gly 225 230 235 240 Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn Leu Pro Phe Gln                 245 250 255 Asn Ile Asn Ser Arg Ala Val Gly Lys Cys Pro Arg Tyr Val Lys             260 265 270 <210> 25 <211> 263 <212> PRT <213> Artificial Sequence <220> <223> A / New York / 107/2003 HA1-1 <400> 25 Glu Thr Val Glu Thr Thr Asn Ile Lys Lys Ile Cys Thr Gln Gly Lys  1 5 10 15 Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Leu Ile Gly             20 25 30 Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ser Asp Leu Ile Ile         35 40 45 Glu Arg Arg Glu Gly Thr Asp Ile Cys Tyr Pro Gly Arg Phe Thr Asn     50 55 60 Glu Glu Ser Leu Arg Gln Ile Leu Arg Arg Ser Gly Gly Ile Gly Lys 65 70 75 80 Glu Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala Thr                 85 90 95 Ser Ala Cys Thr Arg Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys Trp             100 105 110 Leu Leu Ser Asn Ser Asp Asn Ala Phe Pro Gln Met Thr Lys Ala         115 120 125 Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile Ile Trp Gly Val His     130 135 140 His Ser Glu Ser Val Ser Glu Gln Thr Lys Leu Tyr Gly Ser Gly Asn 145 150 155 160 Lys Leu Ile Thr Val Arg Ser Ser Lys Tyr Gln Gln Ser Phe Thr Pro                 165 170 175 Asn Pro Gly Ala Arg Arg Ile Asp Phe His Trp Leu Leu Leu Asp Pro             180 185 190 Asn Asp Thr Val Thr Phe Thr Phe Asn Gly Ala Phe Ile Ala Pro Asp         195 200 205 Arg Thr Ser Phe Phe Arg Gly Glu Ser Leu Gly Val Gln Ser Asp Ala     210 215 220 Pro Leu Asp Ser Ser Cys Arg Gly Asp Cys Phe His Ser Gly Gly Thr 225 230 235 240 Ile Val Ser Ser Leu Pro Phe Gln Asn Ile Asn Ser Arg Thr Val Gly                 245 250 255 Lys Cys Pro Arg Tyr Val Lys             260 <210> 26 <211> 271 <212> PRT <213> Artificial Sequence <220> <223> A / mallard / Netherlands / 12/2000 HA1-1 <400> 26 Glu Thr Val Glu Arg Thr Asn Val Pro Arg Ile Cys Ser Lys Gly Lys  1 5 10 15 Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Ile Thr Gly             20 25 30 Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp Leu Ile Ile         35 40 45 Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys Phe Val Asn     50 55 60 Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly Ile Asp Lys 65 70 75 80 Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala Thr                 85 90 95 Ser Ala Cys Arg Arg Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys Trp             100 105 110 Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met Thr Lys Ser         115 120 125 Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile Trp Gly Ile His     130 135 140 His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr Gly Ser Gly Asn 145 150 155 160 Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser Phe Val Pro                 165 170 175 Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly Arg Ile Asp             180 185 190 Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr Val Thr Phe Ser Phe         195 200 205 Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu Arg Gly Lys     210 215 220 Ser Met Gly Ile Gln Ser Gly Val Gln Val Asp Ala Asn Cys Glu Gly 225 230 235 240 Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn Leu Pro Phe Gln                 245 250 255 Asn Ile Asn Ser Arg Ala Val Gly Lys Cys Pro Arg Tyr Val Lys             260 265 270 <210> 27 <211> 271 <212> PRT <213> Artificial Sequence <220> <223> A / Canada / RV504 / 2004 HA1-1 <400> 27 Glu Thr Val Glu Thr Val Asn Ile Lys Lys Ile Cys Thr Gln Gly Lys  1 5 10 15 Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Leu Ile Gly             20 25 30 Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Asp Ala Asn Leu Ile Ile         35 40 45 Glu Arg Arg Glu Gly Thr Asp Val Cys Tyr Pro Gly Lys Phe Thr Asn     50 55 60 Glu Glu Ser Leu Arg Gln Ile Leu Arg Gly Ser Gly Gly Ile Asp Lys 65 70 75 80 Glu Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala Thr                 85 90 95 Ser Ala Cys Arg Arg Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys Trp             100 105 110 Leu Leu Ser Asn Ser Asp Asn Ala Ala Phe Pro Gln Met Thr Lys Ser         115 120 125 Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile Ile Trp Gly Val His     130 135 140 His Ser Gly Ser Ala Thr Glu Gln Thr Lys Leu Tyr Gly Ser Gly Asn 145 150 155 160 Lys Leu Ile Thr Val Gly Ser Ser Lys Tyr Gln Gln Ser Phe Thr Pro                 165 170 175 Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly Arg Ile Asp             180 185 190 Phe His Trp Leu Leu Leu Asp Pro Asn Asp Thr Val Thr Phe Thr Phe         195 200 205 Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Phe Arg Gly Glu     210 215 220 Ser Leu Gly Val Gln Ser Ser Val Val Pro Leu Asp Ser Gly Cys Glu Gly 225 230 235 240 Asp Cys Phe His Ser Gly Gly Thr Ile Val Ser Ser Leu Pro Phe Gln                 245 250 255 Asn Ile Asn Pro Arg Thr Val Gly Lys Cys Pro Arg Tyr Val Lys             260 265 270 <210> 28 <211> 271 <212> PRT <213> Artificial Sequence <220> <223> A / Netherlands / 219/03 HA1-1 <400> 28 Glu Thr Val Glu Arg Thr Asn Val Pro Arg Ile Cys Ser Lys Gly Lys  1 5 10 15 Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Ile Thr Gly             20 25 30 Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp Leu Ile Ile         35 40 45 Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys Phe Val Asn     50 55 60 Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly Ile Asp Lys 65 70 75 80 Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Thr Thr                 85 90 95 Ser Ala Cys Arg Arg Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys Trp             100 105 110 Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met Thr Lys Ser         115 120 125 Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile Trp Gly Ile His     130 135 140 His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr Gly Ser Gly Asn 145 150 155 160 Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser Phe Val Pro                 165 170 175 Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly Arg Ile Asp             180 185 190 Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr Val Thr Phe Ser Phe         195 200 205 Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu Arg Gly Lys     210 215 220 Ser Met Gly Ile Gln Ser Glu Val Gln Val Asp Ala Asn Cys Glu Gly 225 230 235 240 Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn Leu Pro Phe Gln                 245 250 255 Asn Ile Asn Ser Arg Ala Val Gly Lys Cys Pro Arg Tyr Val Lys             260 265 270 <210> 29 <211> 268 <212> PRT <213> Artificial Sequence <220> <223> A / Hong Kong / 33982/2009 HA1-1 <400> 29 Gln Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn Leu Gly His Pro  1 5 10 15 Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr Gly Asn Pro             20 25 30 Ser Cys Asp Leu Leu Leu Glu Gly Arg Glu Trp Ser Tyr Ile Val Glu         35 40 45 Arg Pro Ser Ala Val Asn Gly Thr Cys Tyr Pro Gly Asn Val Glu Asn     50 55 60 Leu Glu Glu Leu Arg Thr Leu Phe Ser Ser Ala Ser Ser Tyr Gln Arg 65 70 75 80 Ile Gln Ile Phe Pro Asp Thr Thr Trp Asn Val Thr Tyr Thr Gly Thr                 85 90 95 Ser Arg Ser Cys Ser Gly Ser Phe Tyr Arg Ser Met Arg Trp Leu Thr             100 105 110 Gln Lys Ser Gly Phe Tyr Pro Val Gln Asp Ala Lys Tyr Thr Asn Asn         115 120 125 Arg Gly Lys Asn Ile Leu Phe Val Trp Gly Ile His His Pro His Thr     130 135 140 Tyr Thr Asp Gln Thr Thr Leu Tyr Ile Arg Asn Asp Thr Thr Thr Ser 145 150 155 160 Val Thr Thr Glu Glu Leu Asn Arg Ile Phe Lys Pro Val Ile Val Pro                 165 170 175 Arg Leu Leu Val Asn Gly Gln Gln Gly Arg Ile Asp Tyr Tyr Trp Ser             180 185 190 Val Leu Lys Pro Gly Gln Thr Leu Arg Val Ser Ser Asn Gly Asn Leu         195 200 205 Ile Ala Pro Trp Tyr Gly His Val Leu Ser Gly Gly Ser His Gly Arg     210 215 220 Ile Leu Lys Thr Asp Leu Lys Ser Gly Asn Cys Val Val Gln Cys Gln 225 230 235 240 Thr Glu Lys Gly Gly Leu Asn Ser Thr Leu Pro Phe His Asn Ile Ser                 245 250 255 Lys Tyr Ala Phe Gly Thr Cys Pro Lys Tyr Val Lys             260 265 <210> 30 <211> 268 <212> PRT <213> Artificial Sequence <220> <223> A / Hong Kong / 1073/99 HA1-1 <400> 30 His Thr Glu His Asn Gly Met Leu Cys Ala Thr Ser Leu Gly His Pro  1 5 10 15 Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Val Tyr Gly Asn Pro             20 25 30 Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser Tyr Ile Val Glu         35 40 45 Arg Ser Ser Ala Val Asn Gly Thr Cys Tyr Pro Gly Asn Val Glu Asn     50 55 60 Leu Glu Glu Leu Arg Thr Leu Phe Ser Ser Ala Ser Ser Tyr Gln Arg 65 70 75 80 Ile Gln Ile Phe Pro Asp Thr Thr Trp Asn Val Thr Tyr Thr Gly Thr                 85 90 95 Ser Arg Ala Cys Ser Gly Ser Phe Tyr Arg Ser Met Arg Trp Leu Thr             100 105 110 Gln Lys Ser Gly Phe Tyr Pro Val Gln Asp Ala Gln Tyr Thr Asn Asn         115 120 125 Arg Gly Lys Ser Ile Leu Phe Val Trp Gly Ile His His Pro Thr     130 135 140 Tyr Thr Glu Gln Thr Asn Leu Tyr Ile Arg Asn Asp Thr Thr Thr Ser 145 150 155 160 Val Thr Thr Glu Asp Leu Asn Arg Thr Phe Lys Pro Val Ile Gly Pro                 165 170 175 Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile Asp Tyr Tyr Trp Ser             180 185 190 Val Leu Lys Pro Gly Gln Thr Leu Arg Val Ser Ser Asn Gly Asn Leu         195 200 205 Ile Ala Pro Trp Tyr Gly His Val Leu Ser Gly Gly Ser His Gly Arg     210 215 220 Ile Leu Lys Thr Asp Leu Lys Gly Gly Asn Cys Val Val Gln Cys Gln 225 230 235 240 Thr Glu Lys Gly Gly Leu Asn Ser Thr Leu Pro Phe His Asn Ile Ser                 245 250 255 Lys Tyr Ala Phe Gly Thr Cys Pro Lys Tyr Val Arg             260 265 <210> 31 <211> 268 <212> PRT <213> Artificial Sequence <220> <223> A / Chicken / Hong Kong / G9 / 97 HA1-1 <400> 31 His Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn Leu Gly Arg Pro  1 5 10 15 Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr Gly Asn Pro             20 25 30 Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser Tyr Ile Val Glu         35 40 45 Arg Pro Ser Ala Val Asn Gly Met Cys Tyr Pro Gly Asn Val Glu Asn     50 55 60 Leu Glu Glu Leu Arg Ser Phe Phe Ser Ser Ala Ser Ser Tyr Gln Arg 65 70 75 80 Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser Tyr Ser Gly Thr                 85 90 95 Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Met Arg Trp Leu Thr             100 105 110 Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala Gln Tyr Thr Asn Asn         115 120 125 Arg Gly Lys Ser Ile Leu Phe Met Trp Gly Ile Asn His Pro Pro Thr     130 135 140 Asp Thr Ala Gln Thr Asn Leu Tyr Thr Arg Thr Asp Thr Thr Thr Ser 145 150 155 160 Val Ala Thr Glu Asp Ile Asn Arg Thr Phe Lys Pro Val Ile Gly Pro                 165 170 175 Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile Asp Tyr Tyr Trp Ser             180 185 190 Val Leu Lys Pro Gly Gln Thr Leu Arg Val Ser Ser Asn Gly Asn Leu         195 200 205 Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu Ser His Gly Arg     210 215 220 Ile Leu Lys Thr Asp Leu Asn Ser Gly Ser Cys Val Val Gln Cys Gln 225 230 235 240 Thr Glu Arg Gly Gly Leu Asn Thr Thr Leu Pro Phe His Asn Val Ser                 245 250 255 Lys Tyr Ala Phe Gly Asn Cys Pro Lys Tyr Val Gly             260 265 <210> 32 <211> 268 <212> PRT <213> Artificial Sequence <220> <223> A / Chicken / Anhui / AH16 / 2008 HA1-1 <400> 32 His Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn Leu Gly His Pro  1 5 10 15 Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr Gly Asn Pro             20 25 30 Ser Cys Asp Leu Leu Leu Gly Gly Gly Glu Trp Ser Tyr Ile Val Glu         35 40 45 Arg Pro Ser Ala Val Asn Gly Leu Cys Tyr Pro Gly Asn Val Glu Asn     50 55 60 Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ala Ser Ser Tyr Gln Arg 65 70 75 80 Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser Tyr Ser Gly Thr                 85 90 95 Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Met Arg Trp Leu Thr             100 105 110 Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala Gln Tyr Thr Asn Asn         115 120 125 Arg Glu Lys Asn Ile Leu Phe Met Trp Gly Ile Asn Gln Pro Pro Thr     130 135 140 Glu Thr Ala Gln Thr Asn Leu Tyr Thr Arg Thr Asp Thr Thr Thr Ser 145 150 155 160 Val Ala Thr Glu Glu Ile Asn Arg Thr Phe Lys Pro Leu Ile Gly Pro                 165 170 175 Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile Asp Tyr Tyr Trp Ser             180 185 190 Val Leu Lys Pro Gly Gln Thr Leu Arg Ile Arg Ser Asn Gly Asn Leu         195 200 205 Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu Ser His Gly Arg     210 215 220 Ile Leu Lys Thr Asp Leu Lys Arg Gly Ser Cys Thr Val Gln Cys Gln 225 230 235 240 Thr Glu Lys Gly Gly Leu Asn Thr Thr Leu Pro Phe Gln Asn Val Ser                 245 250 255 Lys Tyr Ala Phe Gly Asn Cys Ser Lys Tyr Val Gly             260 265 <210> 33 <211> 268 <212> PRT <213> Artificial Sequence <220> <223> A / Swine / Hong Kong / 9/98 HA1-1 <400> 33 His Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn Leu Gly His Pro  1 5 10 15 Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr Gly Asn Pro             20 25 30 Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser Tyr Ile Val Glu         35 40 45 Arg Pro Ser Ala Val Asn Gly Met Cys Tyr Pro Gly Asn Val Glu Asn     50 55 60 Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ala Ser Ser Tyr Gln Arg 65 70 75 80 Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser Tyr Ser Gly Thr                 85 90 95 Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Met Arg Trp Leu Thr             100 105 110 Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala Gln Tyr Thr Asn Asn         115 120 125 Arg Gly Lys Ser Ile Leu Phe Met Trp Gly Ile Asn His Pro Pro Thr     130 135 140 Asp Thr Val Gln Thr Asn Leu Tyr Thr Arg Thr Asp Thr Thr Thr Ser 145 150 155 160 Val Thr Thr Glu Asp Ile Asn Arg Thr Phe Lys Pro Val Ile Gly Pro                 165 170 175 Arg Pro Leu Val Asn Gly Leu His Gly Arg Ile Asp Tyr Tyr Trp Ser             180 185 190 Val Leu Lys Pro Gly Gln Thr Leu Arg Val Ser Ser Asn Gly Asn Leu         195 200 205 Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu Ser His Gly Arg     210 215 220 Ile Leu Lys Thr Asp Leu Asn Ser Gly Asn Cys Val Val Gln Cys Gln 225 230 235 240 Thr Glu Arg Gly Gly Leu Asn Thr Thr Leu Pro Phe His Asn Val Ser                 245 250 255 Lys Tyr Ala Phe Gly Asn Cys Pro Lys Tyr Val Gly             260 265 <210> 34 <211> 268 <212> PRT <213> Artificial Sequence <220> <223> A / Swine / Guangxi / 58/2005 HA1-1 <400> 34 His Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn Leu Gly Arg Pro  1 5 10 15 Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr Gly Asn Pro             20 25 30 Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser Tyr Ile Val Glu         35 40 45 Arg Ser Ser Ala Val Asn Gly Met Cys Tyr Pro Gly Asn Val Glu Asn     50 55 60 Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ala Ser Ser Tyr Gln Arg 65 70 75 80 Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser Tyr Ser Gly Thr                 85 90 95 Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Met Arg Trp Leu Thr             100 105 110 Gln Lys Asp Asn Ala Tyr Pro Ile Gln Asp Ala Gln Tyr Thr Asn Asn         115 120 125 Arg Gly Arg Ser Ile Leu Phe Met Trp Gly Ile Asn His Pro Pro Thr     130 135 140 Asp Thr Thr Gln Thr Asn Leu Tyr Thr Arg Thr Asp Thr Thr Thr Ser 145 150 155 160 Val Ala Thr Glu Asp Ile Asn Arg Thr Phe Lys Pro Leu Ile Gly Pro                 165 170 175 Arg Pro Leu Val Asn Gly Gln Gln Gly Arg Ile Asp Tyr Tyr Trp Ser             180 185 190 Ile Leu Lys Pro Gly Gln Thr Leu Arg Val Ser Ser Asn Gly Asn Leu         195 200 205 Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu Ser His Gly Arg     210 215 220 Ile Leu Lys Thr Asp Leu Lys Lys Gly Asn Cys Val Val Gln Cys Gln 225 230 235 240 Thr Glu Arg Gly Gly Leu Asn Thr Thr Leu Pro Phe His Asn Val Ser                 245 250 255 Lys Tyr Ala Phe Gly Asn Cys Pro Lys Tyr Ile Gly             260 265 <210> 35 <211> 293 <212> PRT <213> Artificial Sequence <220> <223> B / Shanghai / 361/2002 HA1-1 <400> 35 Thr Thr Thr Pro Ile Lys Ser His Phe Ala Asn Leu Lys Gly Thr Arg  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys         35 40 45 Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu                 85 90 95 Lys Ala Leu Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val     130 135 140 Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe 145 150 155 160 His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser Asn                 165 170 175 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val             180 185 190 Ser Gln Ile Gly Gly Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro         195 200 205 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Pro Gly Lys     210 215 220 Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val 225 230 235 240 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu                 245 250 255 Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys             260 265 270 Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly His Cys         275 280 285 Pro Ile Trp Val Lys     290 <210> 36 <211> 293 <212> PRT <213> Artificial Sequence <220> <223> B / Wisconsin / 1/2010 HA1-1 <400> 36 Thr Thr Pro Thr Lys Ser Tyr Phe Ala Asn Leu Lys Gly Thr Arg  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys         35 40 45 Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu                 85 90 95 Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val     130 135 140 Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe 145 150 155 160 His Ser Asp Asn Lys Thr Gln Met Lys Ser Leu Tyr Gly Asp Ser Asn                 165 170 175 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val             180 185 190 Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro         195 200 205 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys     210 215 220 Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val 225 230 235 240 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu                 245 250 255 Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys             260 265 270 Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys         275 280 285 Pro Ile Trp Val Lys     290 <210> 37 <211> 293 <212> PRT <213> Artificial Sequence <220> <223> B / Sichuan / 379/99 HA1-1 <400> 37 Thr Thr Thr Pro Thr Lys Ser His Phe Ala Asn Leu Lys Gly Thr Lys  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Thr Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Met Cys Val Gly Ile Thr Pro Ser Ala Lys         35 40 45 Ala Ser Ile Leu His Glu Ile Lys Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu Lys Ile Arg Leu Ser Thr Gln Asn Val Ile Asn Ala Glu                 85 90 95 Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Arg Asp Asn Asn Lys Thr Ala Thr Asn Pro Leu Thr Val Glu Val     130 135 140 Pro His Ile Cys Thr Lys Glu Glu Asp Gln Ile Thr Val Trp Gly Phe 145 150 155 160 His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser Asn                 165 170 175 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Ile Thr Thr His Tyr Val             180 185 190 Ser Gln Ile Gly Gly Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro         195 200 205 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Pro Gly Lys     210 215 220 Thr Gly Thr Ile Val Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys Val 225 230 235 240 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu                 245 250 255 Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys             260 265 270 Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys         275 280 285 Pro Ile Trp Val Lys     290 <210> 38 <211> 293 <212> PRT <213> Artificial Sequence <220> <223> B / Hubei-Wujiagang / 158/2009 HA1-1 <400> 38 Thr Thr Pro Thr Lys Ser Tyr Phe Ala Asn Leu Lys Gly Thr Arg  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys         35 40 45 Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu                 85 90 95 Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val     130 135 140 Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe 145 150 155 160 His Ser Asp Asn Lys Asn Gln Met Lys Ser Leu Tyr Gly Asp Ser Asn                 165 170 175 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val             180 185 190 Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro         195 200 205 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys     210 215 220 Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val 225 230 235 240 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu                 245 250 255 Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys             260 265 270 Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys         275 280 285 Pro Ile Trp Val Lys     290 <210> 39 <211> 293 <212> PRT <213> Artificial Sequence <220> <223> B / Texas / 06/2011 HA1-1 <400> 39 Thr Thr Pro Thr Lys Ser Tyr Phe Ala Asn Leu Lys Gly Thr Arg  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys         35 40 45 Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu                 85 90 95 Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val     130 135 140 Pro Tyr Ile Cys Lys Glu Glu Glu Asp Gln Ile Thr Val Trp Gly Phe 145 150 155 160 His Ser Asp Asn Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser Asn                 165 170 175 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val             180 185 190 Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro         195 200 205 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys     210 215 220 Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val 225 230 235 240 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu                 245 250 255 Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys             260 265 270 Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys         275 280 285 Pro Ile Trp Val Lys     290 <210> 40 <211> 294 <212> PRT <213> Artificial Sequence <220> <223> B / Brisbane / 60/2008 HA1-1 <400> 40 Thr Thr Thr Pro Thr Lys Ser His Phe Ala Asn Leu Lys Gly Thr Glu  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg         35 40 45 Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn Ala Glu                 85 90 95 Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu     130 135 140 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly 145 150 155 160 Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser                 165 170 175 Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr             180 185 190 Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu         195 200 205 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly     210 215 220 Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys 225 230 235 240 Val Trp Cys Ala Ser Gly Arg Ser Ser Lys Val Ile Lys Gly Ser Leu Pro                 245 250 255 Leu Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn             260 265 270 Lys Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn         275 280 285 Cys Pro Ile Trp Val Lys     290 <210> 41 <211> 294 <212> PRT <213> Artificial Sequence <220> <223> B / Bangladesh / 5945/2009 HA1-1 <400> 41 Thr Thr Thr Pro Thr Lys Ser His Phe Ala Asn Leu Lys Gly Thr Glu  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg         35 40 45 Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu His Ile Arg Leu Ser Thr Asn Asn Val Ile Asn Ala Glu                 85 90 95 Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu     130 135 140 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly 145 150 155 160 Phe His Ser Asp Asn Glu Ile Gln Met Ala Lys Leu Tyr Gly Asp Ser                 165 170 175 Arg Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr             180 185 190 Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu         195 200 205 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly     210 215 220 Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys 225 230 235 240 Val Trp Cys Ala Ser Gly Arg Ser Ser Lys Val Ile Lys Gly Ser Leu Pro                 245 250 255 Leu Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn             260 265 270 Lys Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn         275 280 285 Cys Pro Ile Trp Val Lys     290 <210> 42 <211> 294 <212> PRT <213> Artificial Sequence <220> <223> B / Ohio / 1/2005 HA1-1 <400> 42 Thr Thr Thr Pro Thr Lys Ser His Phe Ala Asn Leu Lys Gly Thr Lys  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Asn Ile Pro Ser Ala Glu         35 40 45 Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn Ala Glu                 85 90 95 Lys Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asn Asp Asn Asn Lys Thr Ala Thr Asn Ser Leu Thr Ile Glu     130 135 140 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Ile Trp Gly 145 150 155 160 Phe His Ser Asp Ser Glu Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser                 165 170 175 Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr             180 185 190 Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu         195 200 205 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly     210 215 220 Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys 225 230 235 240 Val Trp Cys Ala Ser Gly Arg Ser Ser Lys Val Ile Lys Gly Ser Leu Pro                 245 250 255 Leu Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn             260 265 270 Lys Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn         275 280 285 Cys Pro Ile Trp Val Lys     290 <210> 43 <211> 294 <212> PRT <213> Artificial Sequence <220> <223> B / Hong Kong / 259/2010 HA1-1 <400> 43 Thr Thr Thr Pro Thr Lys Ser His Phe Ala Asn Leu Lys Gly Thr Glu  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Lys Cys Pro Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg         35 40 45 Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn Ala Glu                 85 90 95 Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu     130 135 140 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly 145 150 155 160 Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser                 165 170 175 Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr             180 185 190 Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu         195 200 205 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly     210 215 220 Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys 225 230 235 240 Val Trp Cys Ala Ser Gly Arg Ser Ser Lys Val Ile Lys Gly Ser Leu Pro                 245 250 255 Leu Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn             260 265 270 Lys Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn         275 280 285 Cys Pro Ile Trp Val Lys     290 <210> 44 <211> 294 <212> PRT <213> Artificial Sequence <220> <223> B / Hong Kong / 330/2001 HA1-1 <400> 44 Thr Thr Thr Pro Thr Lys Ser His Phe Ala Asn Leu Lys Gly Thr Lys  1 5 10 15 Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp             20 25 30 Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Asn Ile Pro Ser Ala Lys         35 40 45 Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro     50 55 60 Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg 65 70 75 80 Gly Tyr Glu Arg Ile Arg Leu Ser Asn His Asn Val Ile Asn Ala Glu                 85 90 95 Lys Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro             100 105 110 Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val         115 120 125 Pro Lys Asn Glu Asn Asn Lys Thr Ala Thr Asn Ser Leu Thr Ile Glu     130 135 140 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly 145 150 155 160 Phe His Ser Asp Ser Glu Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser                 165 170 175 Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr             180 185 190 Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu         195 200 205 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly     210 215 220 Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys 225 230 235 240 Val Trp Cys Ala Ser Gly Arg Ser Ser Lys Val Ile Lys Gly Ser Leu Pro                 245 250 255 Leu Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn             260 265 270 Lys Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn         275 280 285 Cys Pro Ile Trp Val Lys     290 <210> 45 <211> 239 <212> PRT <213> Artificial Sequence <220> <223> B / Florida / 4/2006 HA1-2 <400> 45 Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr  1 5 10 15 Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro             20 25 30 Ser Ala Lys Ala Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly         35 40 45 Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn     50 55 60 Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile 65 70 75 80 Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly                 85 90 95 Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala             100 105 110 Trp Ala Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr         115 120 125 Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val     130 135 140 Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly 145 150 155 160 Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr                 165 170 175 His Tyr Val Ser Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly             180 185 190 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys         195 200 205 Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro     210 215 220 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 <210> 46 <211> 248 <212> PRT <213> Artificial Sequence <220> <223> B / Florida / 4/2006 HA1-2 extension <400> 46 Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr  1 5 10 15 Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro             20 25 30 Ser Ala Lys Ala Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly         35 40 45 Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn     50 55 60 Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile 65 70 75 80 Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly                 85 90 95 Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala             100 105 110 Trp Ala Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr         115 120 125 Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val     130 135 140 Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly 145 150 155 160 Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr                 165 170 175 His Tyr Val Ser Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly             180 185 190 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys         195 200 205 Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro     210 215 220 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly Ser 225 230 235 240 Leu Pro Leu Ile Gly Glu Ala Asp                 245 <210> 47 <211> 241 <212> PRT <213> Artificial Sequence <220> <223> B / Brisbane / 60/2008 HA1-2 <400> 47 Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile             20 25 30 Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val 65 70 75 80 Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly      <210> 48 <211> 250 <212> PRT <213> Artificial Sequence <220> <223> B / Brisbane / 60/2008 HA1-2 with extension <400> 48 Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile             20 25 30 Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val 65 70 75 80 Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 250 <210> 49 <211> 240 <212> PRT <213> Artificial Sequence <220> <223> B / Wisconsin / 1/2010 HA1-2 <400> 49 Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met Lys Ser Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 <210> 50 <211> 249 <212> PRT <213> Artificial Sequence <220> <223> B / Wisconsin / 1/2010 HA1-2 with extension <400> 50 Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met Lys Ser Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 <210> 51 <211> 241 <212> PRT <213> Artificial Sequence <220> <223> B / Bangladesh / 5945/2009 HA1-2 <400> 51 Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile             20 25 30 Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr Asn Asn Val 65 70 75 80 Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Asn Glu Ile Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Arg Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly      <210> 52 <211> 250 <212> PRT <213> Artificial Sequence <220> <223> B / Bangladesh / 5945/2009 HA1-2 extension <400> 52 Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile             20 25 30 Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr Asn Asn Val 65 70 75 80 Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Asn Glu Ile Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Arg Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 250 <210> 53 <211> 241 <212> PRT <213> Artificial Sequence <220> <223> B / Hong Kong / 259/2010 HA1-2 <400> 53 Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Pro Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile             20 25 30 Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val 65 70 75 80 Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly      <210> 54 <211> 250 <212> PRT <213> Artificial Sequence <220> <223> B / Hong Kong / 259/2010 HA1-2 extension <400> 54 Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Pro Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile             20 25 30 Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val 65 70 75 80 Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 250 <210> 55 <211> 240 <212> PRT <213> Artificial Sequence <220> <223> B / Sichuan / 379/99 HA1-2 <400> 55 Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Thr Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Ile Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Ile Lys Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Lys Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Arg Asp Asn Asn Lys Thr Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro His Ile Cys Thr Lys Glu Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Ile Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Ile Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 <210> 56 <211> 249 <212> PRT <213> Artificial Sequence <220> <223> B / Sichuan / 379/99 HA1-2 extension <400> 56 Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Thr Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Ile Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Ile Lys Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Lys Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Arg Asp Asn Asn Lys Thr Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro His Ile Cys Thr Lys Glu Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Ile Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Ile Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 <210> 57 <211> 240 <212> PRT <213> Artificial Sequence <220> <223> B / Hubei-Wujiagang / 158/2009 HA1-2 <400> 57 Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asn Lys Asn Gln Met Lys Ser Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 <210> 58 <211> 249 <212> PRT <213> Artificial Sequence <220> <223> B / Hubei-Wujiagang / 158/2009 HA1-2 extension <400> 58 Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asn Lys Asn Gln Met Lys Ser Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 <210> 59 <211> 240 <212> PRT <213> Artificial Sequence <220> <223> B / Texas / 06/2011 HA1-2 <400> 59 Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro Tyr Ile Cys Lys Glu Glu Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met Lys Asn Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 <210> 60 <211> 249 <212> PRT <213> Artificial Sequence <220> <223> B / Texas / 06/2011 HA1-2 extension <400> 60 Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro Tyr Ile Cys Lys Glu Glu Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met Lys Asn Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 <210> 61 <211> 241 <212> PRT <213> Artificial Sequence <220> <223> B / Malaysia / 2506/2004 HA1-2 <400> 61 Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Asn Ile             20 25 30 Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val 65 70 75 80 Ile Asn Ala Glu Asn Ala Pro Gly Gly Ser Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Asn Asn Lys Thr Ala Thr Asn Ser         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Asn Glu Ala Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly      <210> 62 <211> 250 <212> PRT <213> Artificial Sequence <220> <223> B / Malaysia / 2506/2004 HA1-2 extension <400> 62 Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Asn Ile             20 25 30 Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val 65 70 75 80 Ile Asn Ala Glu Asn Ala Pro Gly Gly Ser Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Asn Asn Lys Thr Ala Thr Asn Ser         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Asn Glu Ala Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 250 <210> 63 <211> 223 <212> PRT <213> Artificial Sequence <220> <223> A / Solomon Islands / 3/2006 HA1-2 <400> 63 Lys Gly Ile Ala Pro Leu Gln Leu Gly Asn Cys Ser Val Ala Gly Trp  1 5 10 15 Ile Leu Gly Asn Pro Glu Cys Glu Leu Leu Ile Ser Arg Glu Ser Trp             20 25 30 Ser Tyr Ile Val Glu Lys Pro Asn Pro Glu Asn Gly Thr Cys Tyr Pro         35 40 45 Gly His Phe Ala Asp Tyr Glu Glu Leu Arg Glu Gln Leu Ser Ser Val     50 55 60 Ser Ser Phe Glu Arg Phe Glu Ile Phe Pro Lys Glu Ser Ser Trp Pro 65 70 75 80 Asn His Thr Thr Thr Gly Val Ser Ala Ser Cys Ser His Asn Gly Glu                 85 90 95 Ser Ser Phe Tyr Lys Asn Leu Leu Trp Leu Thr Gly Lys Asn Gly Leu             100 105 110 Tyr Pro Asn Leu Ser Lys Ser Tyr Ala Asn Asn Lys Glu Lys Glu Val         115 120 125 Leu Val Leu Trp Gly Val His His Pro Pro Asn Ile Gly Asp Gln Arg     130 135 140 Ala Leu Tyr His Lys Glu Asn Ala Tyr Val Ser Ser Val Ser Ser His 145 150 155 160 Tyr Ser Arg Lys Phe Thr Pro Glu Ile Ala Lys Arg Pro Lys Val Arg                 165 170 175 Asp Gln Glu Gly Arg Ile Asn Tyr Tyr Trp Thr Leu Leu Glu Pro Gly             180 185 190 Asp Thr Ile Ile Phe Glu Ala Asn Gly Asn Leu Ile Ala Pro Arg Tyr         195 200 205 Ala Phe Ala Leu Ser Arg Gly Phe Gly Ser Gly Ile Ile Asn Ser     210 215 220 <210> 64 <211> 218 <212> PRT <213> Artificial Sequence <220> <223> A / Perth / 16/2009 HA1-2 <400> 64 Ser Pro His Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp Ala  1 5 10 15 Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp             20 25 30 Leu Phe Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp         35 40 45 Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr     50 55 60 Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn 65 70 75 80 Gly Thr Ser Ser Ala Cys Ile Arg Arg Ser Ser Ser Ser Ser Phe Ser Ser                 85 90 95 Arg Leu Asn Trp Leu Thr His Leu Asn Phe Lys Tyr Pro Ala Leu Asn             100 105 110 Val Thr Met Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Ile Trp Gly         115 120 125 Val His His Pro Gly Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln     130 135 140 Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val 145 150 155 160 Ser Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser Arg                 165 170 175 Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile             180 185 190 Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg         195 200 205 Ser Gly Lys Ser Ser Ile Met Arg Ser Serp     210 215 <210> 65 <211> 218 <212> PRT <213> Artificial Sequence <220> <223> A / Wyoming / 03/2003 HA1-2 <400> 65 Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala  1 5 10 15 Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp             20 25 30 Leu Phe Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp         35 40 45 Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr     50 55 60 Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Ala Gly Val Thr Gln Asn 65 70 75 80 Gly Thr Ser Ser Ala Cys Lys Arg Arg Ser Asn Lys Ser Phe Phe Ser                 85 90 95 Arg Leu Asn Trp Leu Thr His Leu Lys Tyr Lys Tyr Pro Ala Leu Asn             100 105 110 Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly         115 120 125 Val His His Pro Val Thr Asp Ser Asp Gln Ile Ser Leu Tyr Ala Gln     130 135 140 Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val 145 150 155 160 Ile Pro Asn Ile Gly Tyr Arg Pro Arg Val Arg Asp Ile Ser Ser Arg                 165 170 175 Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile             180 185 190 Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg         195 200 205 Ser Gly Lys Ser Ser Ile Met Arg Ser Serp     210 215 <210> 66 <211> 218 <212> PRT <213> Artificial Sequence <220> <223> A / New York / 2782/2004 HA1-2 <400> 66 Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala  1 5 10 15 Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp             20 25 30 Leu Phe Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp         35 40 45 Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr     50 55 60 Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn 65 70 75 80 Gly Thr Ser Ser Ala Cys Lys Arg Ser Ser Asn Ser Ser Phe Phe Ser                 85 90 95 Arg Leu Asn Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu Asn             100 105 110 Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly         115 120 125 Val His His Pro Ser Thr Asp Asn Asp Gln Ile Ser Leu Tyr Ala Gln     130 135 140 Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val 145 150 155 160 Ile Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asp Ile Pro Ser Arg                 165 170 175 Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile             180 185 190 Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg         195 200 205 Ser Gly Lys Ser Ser Ile Met Arg Ser Serp     210 215 <210> 67 <211> 218 <212> PRT <213> Artificial Sequence <220> <223> A / Victoria / 361/2011 HA1-2 <400> 67 Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala  1 5 10 15 Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp             20 25 30 Leu Phe Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp         35 40 45 Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr     50 55 60 Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn 65 70 75 80 Gly Thr Ser Ser Ala Cys Ile Arg Ser Ser Asn Ser Ser Phe Ser Ser                 85 90 95 Arg Leu Asn Trp Leu Thr Gln Leu Asn Phe Lys Tyr Pro Ala Leu Asn             100 105 110 Val Thr Met Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Ile Trp Gly         115 120 125 Val His His Pro Val Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln     130 135 140 Ser Ser Gly Arg Ile Thr Ser Ser Thr Lys Ser Ser Gln Gln Ala Val 145 150 155 160 Ile Pro Asn Ile Gly Tyr Arg Pro Arg Ile Arg Asn Ile Pro Ser Arg                 165 170 175 Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile             180 185 190 Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg         195 200 205 Ser Gly Lys Ser Ser Ile Met Arg Ser Serp     210 215 <210> 68 <211> 218 <212> PRT <213> Artificial Sequence <220> <223> A / Aichi / 2/68 HA1-2 <400> 68 Asn Pro His Arg Ile Leu Asp Gly Ile Asp Cys Thr Leu Ile Asp Ala  1 5 10 15 Leu Leu Gly Asp Pro His Cys Asp Val Phe Gln Asn Glu Thr Trp Asp             20 25 30 Leu Phe Val Glu Arg Ser Lys Ala Phe Ser Asn Cys Tyr Pro Tyr Asp         35 40 45 Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr     50 55 60 Leu Glu Phe Ile Thr Glu Gly Phe Thr Trp Thr Gly Val Thr Gln Asn 65 70 75 80 Gly Gly Ser Asn Ala Cys Lys Arg Gly Pro Gly Ser Gly Phe Phe Ser                 85 90 95 Arg Leu Asn Trp Leu Thr Lys Ser Gly Ser Thr Tyr Pro Val Leu Asn             100 105 110 Val Thr Met Pro Asn Asn Asp Asn Phe Asp Lys Leu Tyr Ile Trp Gly         115 120 125 Ile His His Pro Ser Thr Asn Gln Glu Gln Thr Ser Leu Tyr Val Gln     130 135 140 Ala Ser Gly Arg Val Thr Val Ser Thr Arg Arg Ser Gln Gln Thr Ile 145 150 155 160 Ile Pro Asn Ile Gly Ser Arg Pro Trp Val Arg Gly Leu Ser Ser Arg                 165 170 175 Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Val Leu Val Ile             180 185 190 Asn Ser Asn Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Met Arg         195 200 205 Thr Gly Lys Ser Ser Ile Met Arg Ser Asp     210 215 <210> 69 <211> 218 <212> PRT <213> Artificial Sequence <220> <223> A / Wisconsin / 67/2005 HA1-2 <400> 69 Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala  1 5 10 15 Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp             20 25 30 Leu Phe Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp         35 40 45 Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr     50 55 60 Leu Glu Phe Asn Asp Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn 65 70 75 80 Gly Thr Ser Ser Ala Cys Lys Arg Arg Ser Asn Asn Ser Phe Phe Ser                 85 90 95 Arg Leu Asn Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu Asn             100 105 110 Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly         115 120 125 Val His His Pro Gly Thr Asp Asn Asp Gln Ile Phe Leu His Ala Gln     130 135 140 Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val 145 150 155 160 Ile Pro Asn Ile Gly Ser Arg Pro Arg Ile Arg Asn Ile Pro Ser Arg                 165 170 175 Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile             180 185 190 Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg         195 200 205 Ser Gly Lys Ser Ser Ile Met Arg Ser Serp     210 215 <210> 70 <211> 223 <212> PRT <213> Artificial Sequence <220> <223> A / Anhui / 1/2005 HA1-2 <400> 70 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu  1 5 10 15 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser             20 25 30 Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn Asp Leu Cys Tyr Pro Gly         35 40 45 Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn     50 55 60 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His 65 70 75 80 Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly Thr Pro                 85 90 95 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Asn Thr Tyr             100 105 110 Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu         115 120 125 Ile Leu Trp Gly Ile His His Ser Asn Asp Ala Ala Glu Gln Thr Lys     130 135 140 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser Thr Leu 145 150 155 160 Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Val Asn Gly                 165 170 175 Gln Ser Gly Arg Met Asp Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp             180 185 190 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala         195 200 205 Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala Ile Val Lys Ser Glu     210 215 220 <210> 71 <211> 223 <212> PRT <213> Artificial Sequence <220> <223> A / Bar headed goose / Qinghai / 1A / 2005 HA1-2 <400> 71 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu  1 5 10 15 Leu Gly Asn Pro Met Cys Asp Glu Phe Leu Asn Val Pro Glu Trp Ser             20 25 30 Tyr Ile Val Glu Lys Ile Asn Pro Ala Asn Asp Leu Cys Tyr Pro Gly         35 40 45 Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn     50 55 60 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His 65 70 75 80 Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly Arg Ser                 85 90 95 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Asn Ala Tyr             100 105 110 Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu         115 120 125 Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Arg     130 135 140 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser Thr Leu 145 150 155 160 Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Val Asn Gly                 165 170 175 Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp             180 185 190 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Asn Ala         195 200 205 Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu     210 215 220 <210> 72 <211> 223 <212> PRT <213> Artificial Sequence <220> <223> A / Indonesia / 5/2005 HA1-2 <400> 72 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu  1 5 10 15 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser             20 25 30 Tyr Ile Val Glu Lys Ala Asn Pro Thr Asn Leu Cys Tyr Pro Gly         35 40 45 Ser Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn     50 55 60 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His 65 70 75 80 Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Leu Gly Ser Pro                 85 90 95 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser Thr Tyr             100 105 110 Pro Thr Ile Lys Lys Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu         115 120 125 Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Arg     130 135 140 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Ile Gly Thr Ser Thr Leu 145 150 155 160 Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Val Asn Gly                 165 170 175 Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp             180 185 190 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala         195 200 205 Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala Ile Met Lys Ser Glu     210 215 220 <210> 73 <211> 223 <212> PRT <213> Artificial Sequence <220> <223> A / Hubei / 1/2010 / HA1-2 <400> 73 Gly Val Lys Pro Leu Ile Leu Lys Asp Cys Ser Val Ala Gly Trp Leu  1 5 10 15 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser             20 25 30 Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn Asp Leu Cys Tyr Pro Gly         35 40 45 Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn     50 55 60 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Asn Ser Trp Ser Asp His 65 70 75 80 Glu Ala Ser Leu Gly Val Ser Ala Ala Cys Pro Tyr Gln Gly Lys Ser                 85 90 95 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asp Asn Ala Tyr             100 105 110 Pro Thr Ile Lys Lys Gly Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu         115 120 125 Val Leu Trp Gly Ile His His Pro Asn Asp Glu Ala Glu Gln Thr Arg     130 135 140 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Ile Gly Thr Ser Thr Leu 145 150 155 160 Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Ile Asn Gly                 165 170 175 Gln Ser Gly Arg Ile Asp Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp             180 185 190 Ala Ile His Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala         195 200 205 Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu     210 215 220 <210> 74 <211> 223 <212> PRT <213> Artificial Sequence <220> <223> A / Hong Kong / 156/97 HA1-2 <400> 74 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu  1 5 10 15 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser             20 25 30 Tyr Ile Val Glu Lys Ala Ser Pro Ala Asn Asp Leu Cys Tyr Pro Gly         35 40 45 Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn     50 55 60 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asn His 65 70 75 80 Asp Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Leu Gly Arg Ser                 85 90 95 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser Ala Tyr             100 105 110 Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu         115 120 125 Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Lys     130 135 140 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser Thr Leu 145 150 155 160 Asn Gln Arg Leu Val Pro Glu Ile Ala Thr Arg Pro Lys Val Asn Gly                 165 170 175 Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp             180 185 190 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala         195 200 205 Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu     210 215 220 <210> 75 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Anhui / 1/2013 HA1-2 <400> 75 Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Ile Thr  1 5 10 15 Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp Leu Ile             20 25 30 Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys Phe Val         35 40 45 Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly Ile Asp     50 55 60 Lys Glu Ala Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala 65 70 75 80 Thr Ser Ala Cys Arg Ser Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys                 85 90 95 Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met Thr Lys             100 105 110 Ser Tyr Lys Asn Thr Arg Lys Ser Pro Ala Leu Ile Val Trp Gly Ile         115 120 125 His His Ser Val Ser Thr Ala Glu Gln Thr Lys Leu Tyr Gly Ser Gly     130 135 140 Asn Lys Leu Val Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser Phe Val 145 150 155 160 Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Leu Ser Gly Arg Ile                 165 170 175 Asp Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr Val Thr Phe Ser             180 185 190 Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu Arg Gly         195 200 205 Lys Ser Met Gly Ile Gln Ser Gly     210 215 <210> 76 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Turkey / Italy / 214845/2002 HA1-2 <400> 76 Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Ile Thr  1 5 10 15 Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp Leu Ile             20 25 30 Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys Phe Val         35 40 45 Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly Ile Asp     50 55 60 Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala 65 70 75 80 Thr Ser Ala Cys Arg Ser Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys                 85 90 95 Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met Thr Lys             100 105 110 Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile Trp Gly Ile         115 120 125 His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr Gly Ser Gly     130 135 140 Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser Phe Val 145 150 155 160 Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly Arg Ile                 165 170 175 Asp Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr Val Thr Phe Ser             180 185 190 Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu Arg Gly         195 200 205 Lys Ser Met Gly Ile Gln Ser Ser     210 215 <210> 77 <211> 208 <212> PRT <213> Artificial Sequence <220> <223> A / New York / 107/2003 HA1-2 <400> 77 Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Leu Ile  1 5 10 15 Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ser Asp Leu Ile             20 25 30 Ile Glu Arg Arg Glu Gly Thr Asp Ile Cys Tyr Pro Gly Arg Phe Thr         35 40 45 Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg Arg Ser Gly Gly Ile Gly     50 55 60 Lys Glu Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala 65 70 75 80 Thr Ser Ala Cys Thr Arg Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys                 85 90 95 Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala Phe Pro Gln Met Thr Lys             100 105 110 Ala Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile Ile Trp Gly Val         115 120 125 His His Glu Ser Ser Ser Glu Gln Thr Lys Leu Tyr Gly Ser Gly     130 135 140 Asn Lys Leu Ile Thr Val Arg Ser Ser Lys Tyr Gln Gln Ser Phe Thr 145 150 155 160 Pro Asn Pro Gly Ala Arg Arg Ile Asp Phe His Trp Leu Leu Leu Asp                 165 170 175 Pro Asn Asp Thr Val Thr Phe Thr Phe Asn Gly Ala Phe Ile Ala Pro             180 185 190 Asp Arg Thr Ser Phe Phe Arg Gly Glu Ser Leu Gly Val Gln Ser Asp         195 200 205 <210> 78 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Mallard / Netherlands / 12/2000 HA1-2 <400> 78 Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Ile Thr  1 5 10 15 Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp Leu Ile             20 25 30 Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys Phe Val         35 40 45 Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly Ile Asp     50 55 60 Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala 65 70 75 80 Thr Ser Ala Cys Arg Ser Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys                 85 90 95 Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met Thr Lys             100 105 110 Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile Trp Gly Ile         115 120 125 His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr Gly Ser Gly     130 135 140 Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser Phe Val 145 150 155 160 Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly Arg Ile                 165 170 175 Asp Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr Val Thr Phe Ser             180 185 190 Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu Arg Gly         195 200 205 Lys Ser Met Gly Ile Gln Ser Gly     210 215 <210> 79 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Canada / RV504 / 2004 HA1-2 <400> 79 Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Leu Ile  1 5 10 15 Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Asp Ala Asn Leu Ile             20 25 30 Ile Glu Arg Arg Glu Gly Thr Asp Val Cys Tyr Pro Gly Lys Phe Thr         35 40 45 Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg Gly Ser Gly Gly Ile Asp     50 55 60 Lys Glu Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Ala 65 70 75 80 Thr Ser Ala Cys Arg Ser Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys                 85 90 95 Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala Phe Pro Gln Met Thr Lys             100 105 110 Ser Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile Ile Trp Gly Val         115 120 125 His His Ser Gly Ser Ala Thr Glu Gln Thr Lys Leu Tyr Gly Ser Gly     130 135 140 Asn Lys Leu Ile Thr Val Gly Ser Ser Lys Tyr Gln Gln Ser Phe Thr 145 150 155 160 Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly Arg Ile                 165 170 175 Asp Phe His Trp Leu Leu Leu Asp Pro Asn Asp Thr Val Thr Phe Thr             180 185 190 Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Phe Arg Gly         195 200 205 Glu Ser Leu Gly Val Glu Ser Asp     210 215 <210> 80 <211> 223 <212> PRT <213> Artificial Sequence <220> <223> A / Vietnam / 1203/2004 HA1-2 <400> 80 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu  1 5 10 15 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser             20 25 30 Tyr Ile Val Glu Lys Ala Asn Pro Val Asn Asp Leu Cys Tyr Pro Gly         35 40 45 Asp Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn     50 55 60 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Ser His 65 70 75 80 Glu Ala Ser Leu Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly Lys Ser                 85 90 95 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser Thr Tyr             100 105 110 Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu         115 120 125 Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Lys     130 135 140 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser Thr Leu 145 150 155 160 Asn Gln Arg Leu Val Pro Arg Ile Ala Thr Arg Ser Lys Val Asn Gly                 165 170 175 Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp             180 185 190 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala         195 200 205 Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu     210 215 220 <210> 81 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Netherlands / 219/03 HA1-2 <400> 81 Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr Ile Thr  1 5 10 15 Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp Leu Ile             20 25 30 Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys Phe Val         35 40 45 Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly Ile Asp     50 55 60 Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn Gly Thr 65 70 75 80 Thr Ser Ala Cys Arg Ser Ser Gly Ser Ser Phe Tyr Ala Glu Met Lys                 85 90 95 Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met Thr Lys             100 105 110 Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile Trp Gly Ile         115 120 125 His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr Gly Ser Gly     130 135 140 Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser Phe Val 145 150 155 160 Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly Arg Ile                 165 170 175 Asp Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr Val Thr Phe Ser             180 185 190 Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu Arg Gly         195 200 205 Lys Ser Met Gly Ile Gln Ser Glu     210 215 <210> 82 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Hong Kong / 33982/2009 HA1-2 <400> 82 Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr  1 5 10 15 Gly Asn Pro Ser Cys Asp Leu Leu Leu Glu Gly Arg Glu Trp Ser Tyr             20 25 30 Ile Val Glu Arg Pro Ser Ala Val Asn Gly Thr Cys Tyr Pro Gly Asn         35 40 45 Val Glu Asn Leu Glu Glu Leu Arg Thr Leu Phe Ser Ser Ala Ser Ser     50 55 60 Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Thr Trp Asn Val Thr Tyr 65 70 75 80 Thr Gly Thr Ser Arg Ser Ser Cys Ser Gly Ser Phe Tyr Arg Ser Ser Arg                 85 90 95 Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro Val Gln Asp Ala Lys Tyr             100 105 110 Thr Asn Asn Arg Gly Lys Asn Ile Leu Phe Val Trp Gly Ile His His         115 120 125 Pro His Thr Tyr Thr Asp Gln Thr Thr Leu Tyr Ile Arg Asn Asp Thr     130 135 140 Thr Thr Ser Val Thr Thr Glu Glu Leu Asn Arg Ile Phe Lys Pro Val 145 150 155 160 Ile Val Pro Arg Leu Leu Val Asn Gly Gln Gln Gly Arg Ile Asp Tyr                 165 170 175 Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Val Ser Ser             180 185 190 Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Val Leu Ser Gly Gly Ser         195 200 205 His Gly Arg Ile Leu Lys Thr Asp     210 215 <210> 83 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Hong Kong / 1073/99 HA1-2 <400> 83 Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Val Tyr  1 5 10 15 Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser Tyr             20 25 30 Ile Val Glu Arg Ser Ser Ala Val Asn Gly Thr Cys Tyr Pro Gly Asn         35 40 45 Val Glu Asn Leu Glu Glu Leu Arg Thr Leu Phe Ser Ser Ala Ser Ser     50 55 60 Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Thr Trp Asn Val Thr Tyr 65 70 75 80 Thr Gly Thr Ser Arg Ala Cys Ser Gly Ser Phe Tyr Arg Ser Ser Arg                 85 90 95 Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro Val Gln Asp Ala Gln Tyr             100 105 110 Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Val Trp Gly Ile His His         115 120 125 Pro Pro Thr Tyr Thr Glu Gln Thr Asn Leu Tyr Ile Arg Asn Asp Thr     130 135 140 Thr Thr Ser Val Thr Thr Glu Asp Leu Asn Arg Thr Phe Lys Pro Val 145 150 155 160 Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile Asp Tyr                 165 170 175 Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Val Ser Ser             180 185 190 Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Val Leu Ser Gly Gly Ser         195 200 205 His Gly Arg Ile Leu Lys Thr Asp     210 215 <210> 84 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Chicken / Hong Kong / G9 / 97 HA1-2 <400> 84 Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr  1 5 10 15 Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser Tyr             20 25 30 Ile Val Glu Arg Pro Ser Ala Val Asn Gly Met Cys Tyr Pro Gly Asn         35 40 45 Val Glu Asn Leu Glu Glu Leu Arg Ser Phe Phe Ser Ser Ala Ser Ser     50 55 60 Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser Tyr 65 70 75 80 Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Ser Arg                 85 90 95 Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala Gln Tyr             100 105 110 Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Met Trp Gly Ile Asn His         115 120 125 Pro Pro Thr Asp Thr Ala Gln Thr Asn Leu Tyr Thr Arg Thr Asp Thr     130 135 140 Thr Thr Ser Ala Thr Glu Asp Ile Asn Arg Thr Phe Lys Pro Val 145 150 155 160 Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile Asp Tyr                 165 170 175 Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Val Ser Ser             180 185 190 Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu Ser         195 200 205 His Gly Arg Ile Leu Lys Thr Asp     210 215 <210> 85 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Chicken / Anhui / AH16 / 2008 HA1-2 <400> 85 Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr  1 5 10 15 Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Gly Glu Trp Ser Tyr             20 25 30 Ile Val Glu Arg Pro Ser Ala Val Asn Gly Leu Cys Tyr Pro Gly Asn         35 40 45 Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ser Ser Ser     50 55 60 Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser Tyr 65 70 75 80 Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Ser Arg                 85 90 95 Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala Gln Tyr             100 105 110 Thr Asn Asn Arg Glu Lys Asn Ile Leu Phe Met Trp Gly Ile Asn Gln         115 120 125 Pro Pro Thr Glu Thr Ala Gln Thr Asn Leu Tyr Thr Arg Thr Asp Thr     130 135 140 Thr Thr Ser Ala Thr Glu Glu Ile Asn Arg Thr Phe Lys Pro Leu 145 150 155 160 Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile Asp Tyr                 165 170 175 Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Ile Arg Ser Asn             180 185 190 Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu Ser         195 200 205 His Gly Arg Ile Leu Lys Thr Asp     210 215 <210> 86 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Swine / Hong Kong / 9/98 HA1-2 <400> 86 Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr  1 5 10 15 Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser Tyr             20 25 30 Ile Val Glu Arg Pro Ser Ala Val Asn Gly Met Cys Tyr Pro Gly Asn         35 40 45 Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ser Ser Ser     50 55 60 Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser Tyr 65 70 75 80 Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Ser Arg                 85 90 95 Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala Gln Tyr             100 105 110 Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Met Trp Gly Ile Asn His         115 120 125 Pro Pro Thr Asp Thr Val Gln Thr Asn Leu Tyr Thr Arg Thr Asp Thr     130 135 140 Thr Thr Ser Val Thr Thr Glu Asp Ile Asn Arg Thr Phe Lys Pro Val 145 150 155 160 Ile Gly Pro Arg Pro Leu Val Asn Gly Leu His Gly Arg Ile Asp Tyr                 165 170 175 Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Val Ser Ser             180 185 190 Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu Ser         195 200 205 His Gly Arg Ile Leu Lys Thr Asp     210 215 <210> 87 <211> 216 <212> PRT <213> Artificial Sequence <220> <223> A / Swine / Guangxi / 58/2005 HA1-2 <400> 87 Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile Tyr  1 5 10 15 Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser Tyr             20 25 30 Ile Val Glu Arg Ser Ser Ala Val Asn Gly Met Cys Tyr Pro Gly Asn         35 40 45 Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ser Ser Ser     50 55 60 Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser Tyr 65 70 75 80 Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Ser Arg                 85 90 95 Trp Leu Thr Gln Lys Asp Asn Ala Tyr Pro Ile Gln Asp Ala Gln Tyr             100 105 110 Thr Asn Asn Arg Gly Arg Ser Ile Leu Phe Met Trp Gly Ile Asn His         115 120 125 Pro Pro Thr Asp Thr Thr Gln Thr Asn Leu Tyr Thr Arg Thr Asp Thr     130 135 140 Thr Thr Ser Ala Thr Glu Asp Ile Asn Arg Thr Phe Lys Pro Leu 145 150 155 160 Ile Gly Pro Arg Pro Leu Val Asn Gly Gln Gln Gly Arg Ile Asp Tyr                 165 170 175 Tyr Trp Ser Ile Leu Lys Pro Gly Gln Thr Leu Arg Val Val Ser Ser             180 185 190 Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu Ser         195 200 205 His Gly Arg Ile Leu Lys Thr Asp     210 215 <210> 88 <211> 240 <212> PRT <213> Artificial Sequence <220> <223> B / Shanghai / 361/2002 HA1-2 <400> 88 Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asp Ala Glu Lys Ala Leu Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 <210> 89 <211> 249 <212> PRT <213> Artificial Sequence <220> <223> B / Shanghai / 361/2002 HA1-2 extension <400> 89 Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr             20 25 30 Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val 65 70 75 80 Ile Asp Ala Glu Lys Ala Leu Gly Gly Pro Tyr Arg Leu Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu         115 120 125 Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr 145 150 155 160 Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asp Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln         195 200 205 Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly 225 230 235 240 Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 <210> 90 <211> 241 <212> PRT <213> Artificial Sequence <220> <223> B / Ohio / 1/2005 HA1-2 <400> 90 Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Asn Ile             20 25 30 Pro Ser Ala Glu Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val 65 70 75 80 Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Asn Asn Lys Thr Ala Thr Asn Ser         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Ile Trp Gly Phe His Ser Asp Ser Glu Thr Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly      <210> 91 <211> 250 <212> PRT <213> Artificial Sequence <220> <223> B / Ohio / 1/2005 HA1-2 extension <400> 91 Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Asn Ile             20 25 30 Pro Ser Ala Glu Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val 65 70 75 80 Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Asn Asn Lys Thr Ala Thr Asn Ser         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Ile Trp Gly Phe His Ser Asp Ser Glu Thr Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 250 <210> 92 <211> 241 <212> PRT <213> Artificial Sequence <220> <223> B / Hong Kong / 330/2001 HA1-2 <400> 92 Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Asn Ile             20 25 30 Pro Ser Ala Lys Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Arg Ile Arg Leu Ser Asn His Asn Val 65 70 75 80 Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Glu Asn Asn Lys Thr Ala Thr Asn Ser         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Ser Glu Thr Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly      <210> 93 <211> 250 <212> PRT <213> Artificial Sequence <220> <223> B / Hong Kong / 330/2001 HA1-2 extension <400> 93 Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Asn Ile             20 25 30 Pro Ser Ala Lys Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu Arg Ile Arg Leu Ser Asn His Asn Val 65 70 75 80 Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Glu Asn Asn Lys Thr Ala Thr Asn Ser         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Ser Glu Thr Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys 225 230 235 240 Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp                 245 250 <210> 94 <211> 248 <212> PRT <213> Artificial Sequence <220> <223> B / Florida / 4/2006 HA1-2 modified C-terminus <400> 94 Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr  1 5 10 15 Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro             20 25 30 Ser Ala Lys Ala Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly         35 40 45 Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn     50 55 60 Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile 65 70 75 80 Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly                 85 90 95 Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala             100 105 110 Trp Ala Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr         115 120 125 Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val     130 135 140 Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly 145 150 155 160 Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr                 165 170 175 His Tyr Val Ser Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly             180 185 190 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys         195 200 205 Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro     210 215 220 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Val Glu Gly Asp 225 230 235 240 Leu Pro Leu Asp Gly Glu Ala Asp                 245 <210> 95 <211> 249 <212> PRT <213> Artificial Sequence <220> <223> B / Brisbane / 60/2008 HA1-2 modified C-terminus <400> 95 Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr  1 5 10 15 Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro             20 25 30 Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly         35 40 45 Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn     50 55 60 Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile 65 70 75 80 Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly                 85 90 95 Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala             100 105 110 Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu         115 120 125 Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr 145 150 155 160 Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln         195 200 205 Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Val Glu Gly 225 230 235 240 Asp Leu Pro Leu Asp Gly Glu Ala Asp                 245 <210> 96 <211> 250 <212> PRT <213> Artificial Sequence <220> <223> B / Hong Kong / 259/2010 HA1-2 modified C-terminus <400> 96 Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Pro Asn Cys  1 5 10 15 Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile             20 25 30 Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser         35 40 45 Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro     50 55 60 Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val 65 70 75 80 Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser                 85 90 95 Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met             100 105 110 Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro         115 120 125 Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile     130 135 140 Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu 145 150 155 160 Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu             180 185 190 Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val         195 200 205 Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu     210 215 220 Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Glu 225 230 235 240 Gly Asp Leu Pro Leu Asp Gly Glu Ala Asp                 245 250 <210> 97 <211> 249 <212> PRT <213> Artificial Sequence <220> <223> B / Bangladesh / 5945/2009 HA1-2 modified C-terminus <400> 97 Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr  1 5 10 15 Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro             20 25 30 Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly         35 40 45 Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn     50 55 60 Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr Asn Asn Val Ile 65 70 75 80 Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly                 85 90 95 Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala             100 105 110 Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu         115 120 125 Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr     130 135 140 Val Trp Gly Phe His Ser Asp Asn Glu Ile Gln Met Ala Lys Leu Tyr 145 150 155 160 Gly Asp Ser Arg Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr                 165 170 175 Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp             180 185 190 Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln         195 200 205 Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu     210 215 220 Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Val Glu Gly 225 230 235 240 Asp Leu Pro Leu Asp Gly Glu Ala Asp                 245 <210> 98 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Perth / 16/2009 HA1-1L <400> 98 Glu Leu Val Gln Ser Ser Ser Thr Gly Glu Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val         35 40 45 Glu Arg Ser Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ala Cys Ile Arg Arg Ser Lys Asn Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr His Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Ile Trp Gly Val His His     130 135 140 Pro Gly Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ala Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ser Pro Asn                 165 170 175 Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asn             260 265 270 Thr Leu Lys         275 <210> 99 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Wyoming / 03/2003 HA1-1L <400> 99 Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val         35 40 45 Glu Arg Ser Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asn Glu Ser Phe Asn Trp Ala Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ala Cys Lys Arg Arg Ser Asn Lys Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr His Leu Lys Tyr Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly Val His His     130 135 140 Pro Val Thr Asp Ser Asp Gln Ile Ser Leu Tyr Ala Gln Ala Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn                 165 170 175 Ile Gly Tyr Arg Pro Arg Val Arg Asp Ile Ser Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asn             260 265 270 Thr Leu Lys         275 <210> 100 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / New York / 2782/2004 HA1-1L <400> 100 Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val         35 40 45 Glu Arg Ser Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ala Cys Lys Arg Ser Ser Asn Ser Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly Val His His     130 135 140 Pro Ser Thr Asp Asn Asp Gln Ile Ser Leu Tyr Ala Gln Ala Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn                 165 170 175 Ile Gly Ser Arg Pro Arg Val Arg Asp Ile Pro Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asn             260 265 270 Thr Leu Lys         275 <210> 101 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Victoria / 361/2011 HA1-1L <400> 101 Glu Leu Val Gln Asn Ser Ser Ile Gly Glu Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val         35 40 45 Glu Arg Ser Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ala Cys Ile Arg Arg Ser Asn Asn Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr Gln Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Ile Trp Gly Val His His     130 135 140 Pro Val Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ser Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Ala Val Ile Pro Asn                 165 170 175 Ile Gly Tyr Arg Pro Arg Ile Arg Asn Ile Pro Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Ser             260 265 270 Thr Leu Lys         275 <210> 102 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Aichi / 2/68 HA1-1L <400> 102 Glu Leu Val Gln Ser Ser Ser Thr Gly Lys Ile Cys Asn Asn Pro His  1 5 10 15 Arg Ile Leu Asp Gly Ile Asp Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro His Cys Asp Val Phe Gln Asn Glu Thr Trp Asp Leu Phe Val         35 40 45 Glu Arg Ser Lys Ala Phe Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Ile Thr Glu Gly Phe Thr Trp Thr Gly Val Thr Gln Asn Gly Gly Ser                 85 90 95 Asn Cys Lys Arg Gly Pro Gly Ser Gly Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr Lys Ser Gly Ser Thr Tyr Pro Val Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Asp Asn Phe Asp Lys Leu Tyr Ile Trp Gly Ile His His     130 135 140 Pro Ser Thr Asn Gln Glu Gln Thr Ser Leu Tyr Val Gln Ala Ser Gly 145 150 155 160 Arg Val Thr Val Ser Thr Arg Arg Ser Gln Gln Thr Ile Ile Pro Asn                 165 170 175 Ile Gly Ser Arg Pro Trp Val Arg Gly Leu Ser Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Val Leu Val Ile Asn Ser Asn         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Met Arg Thr Gly Lys     210 215 220 Ser Ser Ile Met Ser Ser Asp Ala Pro Ile Asp Thr Cys Ile Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Lys Ile Thr Tyr Gly Ala Cys Pro Lys Tyr Val Lys Gln Asn             260 265 270 Thr Leu Lys         275 <210> 103 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Wisconsin / 67/2005 HA1-1L <400> 103 Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val         35 40 45 Glu Arg Ser Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asp Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ala Cys Lys Arg Arg Ser Asn Asn Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly Val His His     130 135 140 Pro Gly Thr Asp Asn Asp Gln Ile Phe Leu His Ala Gln Ala Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn                 165 170 175 Ile Gly Ser Arg Pro Arg Ile Arg Asn Ile Pro Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asn             260 265 270 Thr Leu Lys         275 <210> 104 <211> 288 <212> PRT <213> Artificial Sequence <220> <223> A / Anhui / 1/2005 HA1-1L <400> 104 His Ala Gln Asp Ile Leu Glu Lys Thr His Asn Gly Lys Leu Cys Asp  1 5 10 15 Leu Asp Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly             20 25 30 Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu         35 40 45 Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn Asp Leu Cys Tyr     50 55 60 Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg 65 70 75 80 Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser                 85 90 95 Asp His Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly             100 105 110 Thr Pro Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Asn         115 120 125 Thr Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp     130 135 140 Leu Leu Ile Leu Trp Gly Ile His His Ser Asn Asp Ala Ala Glu Gln 145 150 155 160 Thr Lys Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser                 165 170 175 Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Val             180 185 190 Asn Gly Gln Ser Gly Arg Met Asp Phe Phe Trp Thr Ile Leu Lys Pro         195 200 205 Asn Asp Ala Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu     210 215 220 Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala Ile Val Lys Ser 225 230 235 240 Glu Val Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Ile Gly                 245 250 255 Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile             260 265 270 Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Lys Leu Val Leu Ala Thr         275 280 285 <210> 105 <211> 288 <212> PRT <213> Artificial Sequence <220> <223> A / Bar headed goose / Qinghai / 1A / 2005 HA1-1L <400> 105 His Ala Gln Asp Ile Leu Glu Lys Thr His Asn Gly Lys Leu Cys Asp  1 5 10 15 Leu Asp Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly             20 25 30 Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Leu Asn Val Pro Glu         35 40 45 Trp Ser Tyr Ile Val Glu Lys Ile Asn Pro Ala Asn Asp Leu Cys Tyr     50 55 60 Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg 65 70 75 80 Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser                 85 90 95 Asp His Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly             100 105 110 Arg Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Asn         115 120 125 Ala Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp     130 135 140 Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln 145 150 155 160 Thr Arg Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser                 165 170 175 Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Val             180 185 190 Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro         195 200 205 Asn Asp Ala Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu     210 215 220 Asn Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser 225 230 235 240 Glu Leu Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Ile Gly                 245 250 255 Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile             260 265 270 Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Arg Leu Val Leu Ala Thr         275 280 285 <210> 106 <211> 288 <212> PRT <213> Artificial Sequence <220> <223> A / Indonesia / 5/2005 HA1-1L <400> 106 His Ala Gln Asp Ile Leu Glu Lys Thr His Asn Gly Lys Leu Cys Asp  1 5 10 15 Leu Asp Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly             20 25 30 Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu         35 40 45 Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Thr Asn Asp Leu Cys Tyr     50 55 60 Pro Gly Ser Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg 65 70 75 80 Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser                 85 90 95 Asp His Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Leu Gly             100 105 110 Ser Pro Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser         115 120 125 Thr Tyr Pro Thr Ile Lys Lys Ser Tyr Asn Asn Thr Asn Gln Glu Asp     130 135 140 Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln 145 150 155 160 Thr Arg Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Ile Gly Thr Ser                 165 170 175 Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Val             180 185 190 Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro         195 200 205 Asn Asp Ala Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu     210 215 220 Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala Ile Met Lys Ser 225 230 235 240 Glu Leu Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Met Gly                 245 250 255 Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile             260 265 270 Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Arg Leu Val Leu Ala Thr         275 280 285 <210> 107 <211> 288 <212> PRT <213> Artificial Sequence <220> <223> A / Vietnam / 1203/2004 HA1-1L <400> 107 His Ala Gln Asp Ile Leu Glu Lys Lys His Asn Gly Lys Leu Cys Asp  1 5 10 15 Leu Asp Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly             20 25 30 Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu         35 40 45 Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Val Asn Asp Leu Cys Tyr     50 55 60 Pro Gly Asp Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg 65 70 75 80 Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser                 85 90 95 Ser His Glu Ala Ser Leu Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly             100 105 110 Lys Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser         115 120 125 Thr Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp     130 135 140 Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln 145 150 155 160 Thr Lys Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser                 165 170 175 Thr Leu Asn Gln Arg Leu Val Pro Arg Ile Ala Thr Arg Ser Ser Val Val             180 185 190 Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro         195 200 205 Asn Asp Ala Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu     210 215 220 Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser 225 230 235 240 Glu Leu Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Met Gly                 245 250 255 Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile             260 265 270 Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Arg Leu Val Leu Ala Thr         275 280 285 <210> 108 <211> 288 <212> PRT <213> Artificial Sequence <220> <223> A / Hubei / 1/2010 HA1-1L <400> 108 His Ala Gln Asp Ile Leu Glu Lys Thr His Asn Gly Lys Leu Cys Asp  1 5 10 15 Leu Asn Gly Val Lys Pro Leu Ile Leu Lys Asp Cys Ser Val Ala Gly             20 25 30 Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu         35 40 45 Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn Asp Leu Cys Tyr     50 55 60 Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg 65 70 75 80 Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Asn Ser Trp Ser                 85 90 95 Asp His Glu Ala Ser Leu Gly Val Ser Ala Ala Cys Pro Tyr Gln Gly             100 105 110 Lys Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asp Asn         115 120 125 Ala Tyr Pro Thr Ile Lys Lys Gly Tyr Asn Asn Thr Asn Gln Glu Asp     130 135 140 Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Glu Ala Glu Gln 145 150 155 160 Thr Arg Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Ile Gly Thr Ser                 165 170 175 Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Ile             180 185 190 Asn Gly Gln Ser Gly Arg Ile Asp Phe Phe Trp Thr Ile Leu Lys Pro         195 200 205 Asn Asp Ala Ile His Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu     210 215 220 Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser 225 230 235 240 Glu Val Glu Tyr Gly Asn Cys Asn Thr Arg Cys Gln Thr Pro Ile Gly                 245 250 255 Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile             260 265 270 Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Lys Leu Val Leu Ala Thr         275 280 285 <210> 109 <211> 288 <212> PRT <213> Artificial Sequence <220> <223> A / Hong Kong / 156/97 HA1-1L <400> 109 His Ala Gln Asp Ile Leu Glu Arg Thr His Asn Gly Lys Leu Cys Asp  1 5 10 15 Leu Asn Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly             20 25 30 Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu         35 40 45 Trp Ser Tyr Ile Val Glu Lys Ala Ser Pro Ala Asn Asp Leu Cys Tyr     50 55 60 Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg 65 70 75 80 Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser                 85 90 95 Asn His Asp Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Leu Gly             100 105 110 Arg Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser         115 120 125 Ala Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp     130 135 140 Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln 145 150 155 160 Thr Lys Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser                 165 170 175 Thr Leu Asn Gln Arg Leu Val Pro Glu Ile Ala Thr Arg Pro Lys Val             180 185 190 Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro         195 200 205 Asn Asp Ala Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu     210 215 220 Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser 225 230 235 240 Glu Leu Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Met Gly                 245 250 255 Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile             260 265 270 Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Arg Leu Val Leu Ala Thr         275 280 285 <210> 110 <211> 282 <212> PRT <213> Artificial Sequence <220> <223> A / Anhui / 1/2013 HA1-1L <400> 110 Asn Ala Thr Glu Thr Val Glu Arg Thr Asn Ile Pro Arg Ile Cys Ser  1 5 10 15 Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr             20 25 30 Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp         35 40 45 Leu Ile Ile Glu Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys     50 55 60 Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly 65 70 75 80 Ile Asp Lys Glu Ala Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn                 85 90 95 Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr Ala Glu             100 105 110 Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met         115 120 125 Thr Lys Ser Tyr Lys Asn Thr Arg Lys Ser Pro Ala Leu Ile Val Trp     130 135 140 Gly Ile His His Ser Val Ser Thr Ala Glu Gln Thr Lys Leu Tyr Gly 145 150 155 160 Ser Gly Asn Lys Leu Val Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser                 165 170 175 Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Leu Ser Gly             180 185 190 Arg Ile Asp Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr Val Thr         195 200 205 Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu     210 215 220 Arg Gly Lys Ser Met Gly Ile Gln Ser Gly Val Gln Val Asp Ala Asn 225 230 235 240 Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn Leu                 245 250 255 Pro Phe Gln Asn Ile Asp Ser Arg Ala Val Gly Lys Cys Pro Arg Tyr             260 265 270 Val Lys Gln Arg Ser Leu Leu Leu Ala Thr         275 280 <210> 111 <211> 282 <212> PRT <213> Artificial Sequence <220> <223> A / Turkey / Italy / 214845/2002 HA1-1L <400> 111 Asn Ala Thr Glu Thr Val Glu Arg Thr Asn Val Pro Arg Ile Cys Ser  1 5 10 15 Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr             20 25 30 Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp         35 40 45 Leu Ile Ile Glu Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys     50 55 60 Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly 65 70 75 80 Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn                 85 90 95 Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr Ala Glu             100 105 110 Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met         115 120 125 Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile Trp     130 135 140 Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr Gly 145 150 155 160 Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser                 165 170 175 Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly             180 185 190 Arg Ile Asp Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr Val Thr         195 200 205 Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu     210 215 220 Arg Gly Lys Ser Met Gly Ile Gln Ser Ser Val Gln Val Asp Ala Asn 225 230 235 240 Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn Leu                 245 250 255 Pro Phe Gln Asn Ile Asn Ser Arg Ala Val Gly Lys Cys Pro Arg Tyr             260 265 270 Val Lys Gln Glu Ser Leu Met Leu Ala Thr         275 280 <210> 112 <211> 274 <212> PRT <213> Artificial Sequence <220> <223> A / New York / 107/2003 HA1-1L <400> 112 Asn Ala Thr Glu Thr Val Glu Thr Thr Asn Ile Lys Lys Ile Cys Thr  1 5 10 15 Gln Gly Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr             20 25 30 Leu Ile Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ser Asp         35 40 45 Leu Ile Ile Glu Arg Glu Gly Thr Asp Ile Cys Tyr Pro Gly Arg     50 55 60 Phe Thr Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg Arg Ser Gly Gly 65 70 75 80 Ile Gly Lys Glu Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn                 85 90 95 Gly Ala Thr Ser Ala Cys Thr Arg Ser Ser Ser Ser Phe Tyr Ala Glu             100 105 110 Met Lys Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala Phe Pro Gln Met         115 120 125 Thr Lys Ala Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile Ile Trp     130 135 140 Gly Val His His Ser Glu Ser Val Ser Glu Gln Thr Lys Leu Tyr Gly 145 150 155 160 Ser Gly Asn Lys Leu Ile Thr Val Arg Ser Ser Lys Tyr Gln Gln Ser                 165 170 175 Phe Thr Pro Asn Pro Gly Ala Arg Arg Ile Asp Phe His Trp Leu Leu             180 185 190 Leu Asp Pro Asn Asp Thr Val Thr Phe Thr Phe Asn Gly Ala Phe Ile         195 200 205 Ala Pro Asp Arg Thr Ser Phe Phe Arg Gly Glu Ser Leu Gly Val Gln     210 215 220 Ser Asp Ala Pro Leu Asp Ser Ser Cys Arg Gly Asp Cys Phe His Ser 225 230 235 240 Gly Gly Thr Ile Val Ser Ser Leu Pro Phe Gln Asn Ile Asn Ser Arg                 245 250 255 Thr Val Gly Lys Cys Pro Arg Tyr Val Lys Gln Lys Ser Leu Leu Leu             260 265 270 Ala Thr          <210> 113 <211> 282 <212> PRT <213> Artificial Sequence <220> <223> A / Mallard / Netherlands / 12/2000 HA1-1L <400> 113 Asn Ala Thr Glu Thr Val Glu Arg Thr Asn Val Pro Arg Ile Cys Ser  1 5 10 15 Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr             20 25 30 Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp         35 40 45 Leu Ile Ile Glu Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys     50 55 60 Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly 65 70 75 80 Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn                 85 90 95 Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr Ala Glu             100 105 110 Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met         115 120 125 Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile Trp     130 135 140 Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr Gly 145 150 155 160 Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser                 165 170 175 Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly             180 185 190 Arg Ile Asp Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr Val Thr         195 200 205 Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu     210 215 220 Arg Gly Lys Ser Met Gly Ile Gln Ser Gly Val Gln Val Asp Ala Asn 225 230 235 240 Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn Leu                 245 250 255 Pro Phe Gln Asn Ile Asn Ser Arg Ala Val Gly Lys Cys Pro Arg Tyr             260 265 270 Val Lys Gln Glu Ser Leu Leu Leu Ala Thr         275 280 <210> 114 <211> 282 <212> PRT <213> Artificial Sequence <220> <223> A / Canada / RV504 / 2004 HA1-1L <400> 114 Asn Ala Thr Glu Thr Val Glu Thr Val Asn Ile Lys Lys Ile Cys Thr  1 5 10 15 Gln Gly Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr             20 25 30 Leu Ile Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Asp Ala Asn         35 40 45 Leu Ile Ile Glu Arg Glu Gly Thr Asp Val Cys Tyr Pro Gly Lys     50 55 60 Phe Thr Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg Gly Ser Gly Gly 65 70 75 80 Ile Asp Lys Glu Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn                 85 90 95 Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr Ala Glu             100 105 110 Met Lys Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala Phe Pro Gln Met         115 120 125 Thr Lys Ser Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile Ile Trp     130 135 140 Gly Val His His Ser Gly Ser Ala Thr Glu Gln Thr Lys Leu Tyr Gly 145 150 155 160 Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Lys Tyr Gln Gln Ser                 165 170 175 Phe Thr Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly             180 185 190 Arg Ile Asp Phe His Trp Leu Leu Leu Asp Pro Asn Asp Thr Val Thr         195 200 205 Phe Thr Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Phe     210 215 220 Arg Gly Glu Ser Leu Gly Val Gln Ser Ser Val Val Pro Leu Asp Ser Gly 225 230 235 240 Cys Glu Gly Asp Cys Phe His Ser Gly Gly Thr Ile Val Ser Ser Leu                 245 250 255 Pro Phe Gln Asn Ile Asn Pro Arg Thr Val Gly Lys Cys Pro Arg Tyr             260 265 270 Val Lys Gln Thr Ser Leu Leu Leu Ala Thr         275 280 <210> 115 <211> 282 <212> PRT <213> Artificial Sequence <220> <223> A / Netherlands / 219/03 HA1-1L <400> 115 Asn Ala Thr Glu Thr Val Glu Arg Thr Asn Val Pro Arg Ile Cys Ser  1 5 10 15 Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly Thr             20 25 30 Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala Asp         35 40 45 Leu Ile Ile Glu Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly Lys     50 55 60 Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly Gly 65 70 75 80 Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr Asn                 85 90 95 Gly Thr Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr Ala Glu             100 105 110 Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln Met         115 120 125 Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile Trp     130 135 140 Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr Gly 145 150 155 160 Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln Ser                 165 170 175 Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser Gly             180 185 190 Arg Ile Asp Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr Val Thr         195 200 205 Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe Leu     210 215 220 Arg Gly Lys Ser Met Gly Ile Gln Ser Glu Val Gln Val Asp Ala Asn 225 230 235 240 Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn Leu                 245 250 255 Pro Phe Gln Asn Ile Asn Ser Arg Ala Val Gly Lys Cys Pro Arg Tyr             260 265 270 Val Lys Gln Glu Ser Leu Leu Leu Ala Thr         275 280 <210> 116 <211> 280 <212> PRT <213> Artificial Sequence <220> <223> A / Hong Kong / 33982/2009 HA1-1L <400> 116 Ala Lys Glu Leu Leu Gln Thr Glu His Asn Gly Met Leu Cys Ala Thr  1 5 10 15 Asn Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu             20 25 30 Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Glu Gly Arg Glu Trp         35 40 45 Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Thr Cys Tyr Pro     50 55 60 Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Thr Leu Phe Ser Ser Ala 65 70 75 80 Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Thr Trp Asn Val                 85 90 95 Thr Tyr Thr Gly Thr Ser Arg Ser Cys Ser Gly Ser Phe Tyr Arg Ser             100 105 110 Met Arg Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro Val Gln Asp Ala         115 120 125 Lys Tyr Thr Asn Asn Arg Gly Lys Asn Ile Leu Phe Val Trp Gly Ile     130 135 140 His His Pro His Thr Tyr Thr Asp Gln Thr Thr Leu Tyr Ile Arg Asn 145 150 155 160 Asp Thr Thr Ser Val Thr Thr Glu Glu Leu Asn Arg Ile Phe Lys                 165 170 175 Pro Val Ile Val Pro Arg Leu Leu Val Asn Gly Gln Gln Gly Arg Ile             180 185 190 Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Arg         195 200 205 Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Val Leu Ser Gly     210 215 220 Gly Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys Ser Gly Asn Cys 225 230 235 240 Val Val Gln Cys Gln Thr Glu Lys Gly Gly Leu Asn Ser Thr Leu Pro                 245 250 255 Phe His Asn Ile Ser Lys Tyr Ala Phe Gly Thr Cys Pro Lys Tyr Val             260 265 270 Lys Val Asn Ser Leu Lys Leu Ala         275 280 <210> 117 <211> 280 <212> PRT <213> Artificial Sequence <220> <223> A / Hong Kong / 1073/99 HA1-1L <400> 117 Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met Leu Cys Ala Thr  1 5 10 15 Ser Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu             20 25 30 Val Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp         35 40 45 Ser Tyr Ile Val Glu Arg Ser Ser Ala Val Asn Gly Thr Cys Tyr Pro     50 55 60 Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Thr Leu Phe Ser Ser Ala 65 70 75 80 Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Thr Trp Asn Val                 85 90 95 Thr Tyr Thr Gly Thr Ser Arg Ala Cys Ser Gly Ser Phe Tyr Arg Ser             100 105 110 Met Arg Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro Val Gln Asp Ala         115 120 125 Gln Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Val Trp Gly Ile     130 135 140 His His Pro Thr Tyr Thr Glu Gln Thr Asn Leu Tyr Ile Arg Asn 145 150 155 160 Asp Thr Thr Thr Ser Val Thr Thr Glu Asp Leu Asn Arg Thr Phe Lys                 165 170 175 Pro Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile             180 185 190 Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Arg         195 200 205 Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Val Leu Ser Gly     210 215 220 Gly Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys Gly Gly Asn Cys 225 230 235 240 Val Val Gln Cys Gln Thr Glu Lys Gly Gly Leu Asn Ser Thr Leu Pro                 245 250 255 Phe His Asn Ile Ser Lys Tyr Ala Phe Gly Thr Cys Pro Lys Tyr Val             260 265 270 Arg Val Asn Ser Leu Lys Leu Ala         275 280 <210> 118 <211> 280 <212> PRT <213> Artificial Sequence <220> <223> A / Chicken / Hong Kong / G9 / 97 HA1-1L <400> 118 Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met Leu Cys Ala Thr  1 5 10 15 Asn Leu Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu             20 25 30 Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp         35 40 45 Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Met Cys Tyr Pro     50 55 60 Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Phe Ser Ser Ala 65 70 75 80 Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val                 85 90 95 Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser             100 105 110 Met Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala         115 120 125 Gln Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Met Trp Gly Ile     130 135 140 Asn His Pro Pro Thr Asp Thr Ala Gln Thr Asn Leu Tyr Thr Arg Thr 145 150 155 160 Asp Thr Thr Thr Ser Val Ala Thr Glu Asp Ile Asn Arg Thr Phe Lys                 165 170 175 Pro Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile             180 185 190 Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Arg         195 200 205 Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly     210 215 220 Glu Ser His Gly Arg Ile Leu Lys Thr Asp Leu Asn Ser Gly Ser Cys 225 230 235 240 Val Val Gln Cys Gln Thr Glu Arg Gly Gly Leu Asn Thr Thr Leu Pro                 245 250 255 Phe His Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys Pro Lys Tyr Val             260 265 270 Gly Val Lys Ser Leu Lys Leu Ala         275 280 <210> 119 <211> 280 <212> PRT <213> Artificial Sequence <220> <223> A / Chicken / Anhui / AH16 / 2008 HA1-1L <400> 119 Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met Leu Cys Ala Thr  1 5 10 15 Asn Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu             20 25 30 Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Gly Glu Trp         35 40 45 Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Leu Cys Tyr Pro     50 55 60 Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ala 65 70 75 80 Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val                 85 90 95 Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser             100 105 110 Met Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala         115 120 125 Gln Tyr Thr Asn Asn Arg Glu Lys Asn Ile Leu Phe Met Trp Gly Ile     130 135 140 Asn Gln Pro Pro Thr Glu Thr Ala Gln Thr Asn Leu Tyr Thr Arg Thr 145 150 155 160 Asp Thr Thr Thr Ser Val Ala Thr Glu Glu Ile Asn Arg Thr Phe Lys                 165 170 175 Pro Leu Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile             180 185 190 Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Ile Arg         195 200 205 Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly     210 215 220 Glu Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys Arg Gly Ser Cys 225 230 235 240 Thr Val Gln Cys Gln Thr Glu Lys Gly Gly Leu Asn Thr Thr Leu Pro                 245 250 255 Phe Gln Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys Ser Lys Tyr Val             260 265 270 Gly Ile Lys Ser Leu Lys Leu Ala         275 280 <210> 120 <211> 280 <212> PRT <213> Artificial Sequence <220> <223> A / Swine / Hong Kong / 9/98 HA1-1L <400> 120 Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met Leu Cys Ala Thr  1 5 10 15 Asn Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu             20 25 30 Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp         35 40 45 Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Met Cys Tyr Pro     50 55 60 Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ala 65 70 75 80 Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val                 85 90 95 Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser             100 105 110 Met Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala         115 120 125 Gln Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Met Trp Gly Ile     130 135 140 Asn His Pro Pro Thr Asp Thr Val Gln Thr Asn Leu Tyr Thr Arg Thr 145 150 155 160 Asp Thr Thr Thr Ser Val Thr Thr Glu Asp Ile Asn Arg Thr Phe Lys                 165 170 175 Pro Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu His Gly Arg Ile             180 185 190 Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Arg         195 200 205 Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly     210 215 220 Glu Ser His Gly Arg Ile Leu Lys Thr Asp Leu Asn Ser Gly Asn Cys 225 230 235 240 Val Val Gln Cys Gln Thr Glu Arg Gly Gly Leu Asn Thr Thr Leu Pro                 245 250 255 Phe His Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys Pro Lys Tyr Val             260 265 270 Gly Val Lys Ser Leu Lys Leu Ala         275 280 <210> 121 <211> 280 <212> PRT <213> Artificial Sequence <220> <223> A / Swine / Guangxi / 58/2005 HA1-1L <400> 121 Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met Leu Cys Ala Thr  1 5 10 15 Asn Leu Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu             20 25 30 Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp         35 40 45 Ser Tyr Ile Val Glu Arg Ser Ser Ala Val Asn Gly Met Cys Tyr Pro     50 55 60 Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ala 65 70 75 80 Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val                 85 90 95 Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser             100 105 110 Met Arg Trp Leu Thr Gln Lys Asp Asn Ala Tyr Pro Ile Gln Asp Ala         115 120 125 Gln Tyr Thr Asn Asn Arg Gly Arg Ser Ile Leu Phe Met Trp Gly Ile     130 135 140 Asn His Pro Thr Asp Thr Thr Gln Thr Asn Leu Tyr Thr Arg Thr 145 150 155 160 Asp Thr Thr Thr Ser Val Ala Thr Glu Asp Ile Asn Arg Thr Phe Lys                 165 170 175 Pro Leu Ile Gly Pro Arg Pro Leu Val Asn Gly Gln Gln Gly Arg Ile             180 185 190 Asp Tyr Tyr Trp Ser Ile Leu Lys Pro Gly Gln Thr Leu Arg Val Arg         195 200 205 Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly     210 215 220 Glu Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys Lys Gly Asn Cys 225 230 235 240 Val Val Gln Cys Gln Thr Glu Arg Gly Gly Leu Asn Thr Thr Leu Pro                 245 250 255 Phe His Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys Pro Lys Tyr Ile             260 265 270 Gly Val Lys Ser Leu Lys Leu Ala         275 280 <210> 122 <211> 644 <212> PRT <213> Artificial Sequence <220> <223> HL098 R3.HA1-2 FL4 <400> 122 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Ser Thr             180 185 190 Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu         195 200 205 Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala     210 215 220 Lys Ala Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly Cys Phe 225 230 235 240 Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu                 245 250 255 Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala             260 265 270 Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys         275 280 285 Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala Trp Ala     290 295 300 Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr Val Glu 305 310 315 320 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly                 325 330 335 Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser             340 345 350 Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr         355 360 365 Val Ser Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu     370 375 380 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly 385 390 395 400 Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys                 405 410 415 Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Ser Val Val             420 425 430 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr         435 440 445 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn     450 455 460 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr 465 470 475 480 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr                 485 490 495 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln             500 505 510 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys         515 520 525 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro     530 535 540 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys 545 550 555 560 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly                 565 570 575 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr             580 585 590 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr         595 600 605 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala     610 615 620 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu 625 630 635 640 Ser Leu Leu Arg                  <210> 123 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> B / FL / 4/2006 HA peptide <400> 123 Ser Leu Pro Leu Ile Gly Glu Ala Asp  1 5 <210> 124 <211> 584 <212> PRT <213> Artificial Sequence <220> <223> Influenza B / Florida / 4/2006 HA <400> 124 Met Lys Ala Ile Ile Val Leu Leu Met Val Val Thr Ser Asn Ala Asp  1 5 10 15 Arg Ile Cys Thr Gly Ile Thr Ser Ser Asn Ser Pro His Val Val Lys             20 25 30 Thr Ala Thr Gln Gly Glu Val Asn Val Thr Gly Val Ile Pro Leu Thr         35 40 45 Thr Thr Pro Thr Lys Ser Tyr Phe Ala Asn Leu Lys Gly Thr Arg Thr     50 55 60 Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val 65 70 75 80 Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala                 85 90 95 Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly Cys Phe Pro Ile             100 105 110 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly         115 120 125 Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys     130 135 140 Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn 145 150 155 160 Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Ala Trp Ala Val Pro                 165 170 175 Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro             180 185 190 Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His         195 200 205 Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser Asn Pro     210 215 220 Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser 225 230 235 240 Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln                 245 250 255 Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr             260 265 270 Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp         275 280 285 Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile     290 295 300 Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys Ser 305 310 315 320 Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys Pro                 325 330 335 Ile Trp Val Lys Thr Pro Leu Lys Leu Ala Asn Gly Thr Lys Tyr Arg             340 345 350 Pro Pro Ala Lys Leu Leu Lys Glu Arg Gly Phe Phe Gly Ala Ile Ala         355 360 365 Gly Phe Leu Glu Gly Gly Trp Glu Gly Met Ile Ala Gly Trp His Gly     370 375 380 Tyr Thr Ser His Gly Ala His Gly Val Ala Val Ala Ala Asp Leu Lys 385 390 395 400 Ser Thr Gln Glu Ala Ile Asn Lys Ile Thr Lys Asn Leu Asn Ser Leu                 405 410 415 Ser Glu Leu Glu Val Lys Asn Leu Gln Arg Leu Ser Gly Ala Met Asp             420 425 430 Glu Leu His Asn Glu Ile Leu Glu Leu Asp Glu Lys Val Asp Asp Leu         435 440 445 Arg Ala Asp Thr Ile Ser Ser Gln Ile Glu Leu Ala Val Leu Leu Ser     450 455 460 Asn Glu Gly Ile Asle Ser Glu Asp Glu His Leu Leu Ala Leu Glu 465 470 475 480 Arg Lys Leu Lys Lys Met Leu Gly Pro Ser Ala Val Glu Ile Gly Asn                 485 490 495 Gly Cys Phe Glu Thr Lys His Lys Cys Asn Gln Thr Cys Leu Asp Arg             500 505 510 Ile Ala Gly Thr Phe Asn Ala Gly Glu Phe Ser Leu Pro Thr Phe         515 520 525 Asp Ser Leu Asn Ile Thr Ala Ala Ser Leu Asn Asp Asp Gly Leu Asp     530 535 540 Asn His Thr Ile Leu Leu Tyr Tyr Ser Thr Ala Ala Ser Ser Leu Ala 545 550 555 560 Val Thr Leu Met Leu Ala Ile Phe Ile Val Tyr Met Val Ser Ser Asp                 565 570 575 Asn Val Ser Cys Ser Ile Cys Leu             580 <210> 125 <211> 652 <212> PRT <213> Artificial Sequence <220> <223> HL352 STF2.R3.HA 1-2 FL4 <400> 125 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Gly Thr             180 185 190 Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu         195 200 205 Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala     210 215 220 Lys Ala Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly Cys Phe 225 230 235 240 Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu                 245 250 255 Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala             260 265 270 Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys         275 280 285 Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala Trp Ala     290 295 300 Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr Val Glu 305 310 315 320 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly                 325 330 335 Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser             340 345 350 Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr         355 360 365 Val Ser Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu     370 375 380 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly 385 390 395 400 Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys                 405 410 415 Val Trp Cys Ala Ser Gly Arg Ser Ser Lys Val Ile Lys Gly Ser Leu Pro             420 425 430 Leu Ile Gly Glu Ala Asp Val Val Ser Ala Asp Ala Lys Asn Ala Leu         435 440 445 Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val     450 455 460 Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr 465 470 475 480 Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala                 485 490 495 Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly             500 505 510 Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr         515 520 525 Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala     530 535 540 Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys 545 550 555 560 Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val                 565 570 575 Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser             580 585 590 Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg         595 600 605 Ser Arg Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser     610 615 620 Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala 625 630 635 640 Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 645 650 <210> 126 <211> 752 <212> PRT <213> Artificial Sequence <220> <223> HL772 STF2.D3Ins.HA 1-2 WI1 D3I-o1 <400> 126 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys     290 295 300 Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser             340 345 350 Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg         355 360 365 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala 385 390 395 400 Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu                 405 410 415 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met             420 425 430 Lys Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala         435 440 445 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp     450 455 460 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp 465 470 475 480 Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg                 485 490 495 Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser             500 505 510 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys Thr         515 520 525 Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala     530 535 540 Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly 545 550 555 560 Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile                 565 570 575 Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp             580 585 590 Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr         595 600 605 Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val     610 615 620 Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala 625 630 635 640 Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu                 645 650 655 Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala             660 665 670 Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn         675 680 685 Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu     690 695 700 Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val 705 710 715 720 Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val                 725 730 735 Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg             740 745 750 <210> 127 <211> 503 <212> PRT <213> Artificial Sequence <220> <223> Flagellin used for fusion proteins with D3I-o1       insert <400> 127 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro         275 280 285 Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val     290 295 300 Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr 305 310 315 320 Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly                 325 330 335 Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys             340 345 350 Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala         355 360 365 Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile     370 375 380 Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys 385 390 395 400 Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro                 405 410 415 Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser             420 425 430 Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu         435 440 445 Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp     450 455 460 Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu 465 470 475 480 Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln                 485 490 495 Asn Val Leu Ser Leu Leu Arg             500 <210> 128 <211> 753 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 BR60 D3I-o1 <400> 128 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys     290 295 300 Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser             340 345 350 Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys         355 360 365 Ile Gly Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr 385 390 395 400 Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly                 405 410 415 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln             420 425 430 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser         435 440 445 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro     450 455 460 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val 465 470 475 480 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln                 485 490 495 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser             500 505 510 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys         515 520 525 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp     530 535 540 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn 545 550 555 560 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr                 565 570 575 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala             580 585 590 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr         595 600 605 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly     610 615 620 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn 625 630 635 640 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala                 645 650 655 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala             660 665 670 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln         675 680 685 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn     690 695 700 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu 705 710 715 720 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser                 725 730 735 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu             740 745 750 Arg      <210> 129 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L PE16 D3I-o1 with mutation <400> 129 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Glu Ile Cys         275 280 285 Asp Ser Pro His Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp 305 310 315 320 Asp Leu Tyr Val Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln         355 360 365 Asn Gly Thr Ser Ser Ala Cys Ile Arg Ser Ser Lys Asn Ser Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr His Leu Asn Phe Lys Tyr Pro Ala Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Val Trp                 405 410 415 Gly Val His His Pro Gly Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala             420 425 430 Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr         435 440 445 Val Ser Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu 465 470 475 480 Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile                 485 490 495 Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys             500 505 510 Cys Asn Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr     530 535 540 Val Lys Gln Asp Thr Leu Glu Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 130 <211> 785 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L AH1 D3I-o1 <400> 130 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Asn Ala Thr Glu Thr Val Glu Arg Thr Asn Ile Pro         275 280 285 Arg Ile Cys Ser Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly     290 295 300 Leu Leu Gly Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu 305 310 315 320 Phe Ser Ala Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys                 325 330 335 Tyr Pro Gly Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg             340 345 350 Glu Ser Gly Gly Ile Asp Lys Glu Ala Met Gly Phe Thr Tyr Ser Gly         355 360 365 Ile Arg Thr Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Gly Ser Ser     370 375 380 Phe Tyr Ala Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala 385 390 395 400 Phe Pro Gln Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Ser Pro Ala                 405 410 415 Leu Ile Val Trp Gly Ile His His Ser Val Ser Thr Ala Glu Gln Thr             420 425 430 Lys Leu Tyr Gly Ser Gly Asn Lys Leu Val Thr Val Gly Ser Ser Asn         435 440 445 Tyr Gln Gln Ser Phe Val Ser Ser Pro Gly Ala Arg Pro Gln Val Asn     450 455 460 Gly Leu Ser Gly Arg Ile Asp Phe His Trp Leu Met Leu Asn Pro Asn 465 470 475 480 Asp Thr Val Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg                 485 490 495 Ala Ser Phe Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Gly Val Gln             500 505 510 Val Asp Ala Asn Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile         515 520 525 Ile Ser Asn Leu Pro Phe Gln Asn Ile Asp Ser Arg Ala Val Gly Lys     530 535 540 Cys Pro Arg Tyr Val Lys Gln Arg Ser Leu Leu Leu Ala Thr Thr Lys 545 550 555 560 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp                 565 570 575 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn             580 585 590 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr         595 600 605 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala     610 615 620 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr 625 630 635 640 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly                 645 650 655 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn             660 665 670 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala         675 680 685 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala     690 695 700 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln 705 710 715 720 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn                 725 730 735 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu             740 745 750 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser         755 760 765 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu     770 775 780 Arg 785 <210> 131 <211> 4 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FljB) <400> 131 Val Thr Leu Ala  One <210> 132 <211> 5 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FljB) <400> 132 Glu Val Asn Val Ala  1 5 <210> 133 <211> 8 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FljB) <400> 133 Lys Tyr Phe Val Thr Ile Gly Gly  1 5 <210> 134 <211> 6 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FliC) <400> 134 Val Leu Thr Ala Asn Ile  1 5 <210> 135 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FliC) <400> 135 Glu Leu Ala Lys Leu Ala Ile Lys Leu  1 5 <210> 136 <211> 4 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FliC) <400> 136 Ile Glu Tyr Lys  One <210> 137 <211> 5 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FliC) <400> 137 Thr Val Ser Leu Ala  1 5 <210> 138 <211> 7 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FliC) <400> 138 Leu Gly Ile Thr Ala Ser Ile  1 5 <210> 139 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FliC) <400> 139 Ser Leu Asn Phe Asp Val Thr Val Gly  1 5 <210> 140 <211> 4 <212> PRT <213> Artificial Sequence <220> <223> Peptide from flagellin (FliC) <400> 140 Thr Val Phe Thr  One <210> 141 <211> 628 <212> PRT <213> Artificial Sequence <220> <223> HL092 STF2.R3-HA 1-2 PR8 <400> 141 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Lys Gly             180 185 190 Ile Ala Pro Leu Gln Leu Gly Lys Cys Asn Ile Ala Gly Trp Leu Leu         195 200 205 Gly Asn Pro Glu Cys Asp Pro Leu Leu Pro Val Arg Ser Serp Ser Tyr     210 215 220 Ile Val Glu Thr Pro Asn Ser Glu Asn Gly Ile Cys Tyr Pro Gly Asp 225 230 235 240 Phe Ile Asp Tyr Glu Glu Leu Arg Glu Gln Leu Ser Ser Val Ser Ser                 245 250 255 Phe Glu Arg Phe Glu Ile Phe Pro Lys Glu Ser Ser Trp Pro Asn His             260 265 270 Asn Thr Asn Gly Val Thr Ala Ala Cys Ser His Glu Gly Lys Ser Ser         275 280 285 Phe Tyr Arg Asn Leu Leu Trp Leu Thr Glu Lys Glu Gly Ser Tyr Pro     290 295 300 Lys Leu Lys Asn Ser Tyr Val Asn Lys Lys Gly Lys Glu Val Leu Val 305 310 315 320 Leu Trp Gly Ile His His Pro Pro Asn Ser Lys Glu Gln Gln Asn Leu                 325 330 335 Tyr Gln Asn Glu Asn Ala Tyr Val Ser Val Val Thr Ser Asn Tyr Asn             340 345 350 Arg Arg Phe Thr Pro Glu Ile Ala Glu Arg Pro Lys Val Arg Asp Gln         355 360 365 Ala Gly Arg Met Met Asn Tyr Tyr Trp Thr Leu Leu Lys Pro Gly Asp Thr     370 375 380 Ile Ile Phe Glu Ala Asn Gly Asn Leu Ile Ala Pro Met Tyr Ala Phe 385 390 395 400 Ala Leu Ser Arg Gly Phe Gly Ser Gly Ile Ile Thr Ser Ser Val Val                 405 410 415 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr             420 425 430 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn         435 440 445 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr     450 455 460 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr 465 470 475 480 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln                 485 490 495 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys             500 505 510 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro         515 520 525 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys     530 535 540 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly 545 550 555 560 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr                 565 570 575 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr             580 585 590 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala         595 600 605 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu     610 615 620 Ser Leu Leu Ala 625 <210> 142 <211> 628 <212> PRT <213> Artificial Sequence <220> <223> HL064 STF2.R3.HA1-2 SI3 <400> 142 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Lys Gly             180 185 190 Ile Ala Pro Leu Gln Leu Gly Asn Cys Ser Val Ala Gly Trp Ile Leu         195 200 205 Gly Asn Pro Glu Cys Glu Leu Leu Ile Ser Arg Glu Ser Trp Ser Tyr     210 215 220 Ile Val Glu Lys Pro Asn Pro Glu Asn Gly Thr Cys Tyr Pro Gly His 225 230 235 240 Phe Ala Asp Tyr Glu Glu Leu Arg Glu Gln Leu Ser Ser Val Ser Ser                 245 250 255 Phe Glu Arg Phe Glu Ile Phe Pro Lys Glu Ser Ser Trp Pro Asn His             260 265 270 Thr Thr Gly Val Ser Ala Ser Cys Ser His Asn Gly Glu Ser Ser         275 280 285 Phe Tyr Lys Asn Leu Leu Trp Leu Thr Gly Lys Asn Gly Leu Tyr Pro     290 295 300 Asn Leu Ser Lys Ser Tyr Ala Asn Asn Lys Glu Lys Glu Val Leu Val 305 310 315 320 Leu Trp Gly Val His His Pro Pro Asn Ile Gly Asp Gln Arg Ala Leu                 325 330 335 Tyr His Lys Glu Asn Ala Tyr Val Ser Val Val Ser Ser His Tyr Ser             340 345 350 Arg Lys Phe Thr Pro Glu Ile Ala Lys Arg Pro Lys Val Arg Asp Gln         355 360 365 Glu Gly Arg Ile Asn Tyr Tyr Trp Thr Leu Leu Glu Pro Gly Asp Thr     370 375 380 Ile Ile Phe Glu Ala Asn Gly Asn Leu Ile Ala Pro Arg Tyr Ala Phe 385 390 395 400 Ala Leu Ser Arg Gly Phe Gly Ser Gly Ile Ile Asn Ser Ser Val Val                 405 410 415 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr             420 425 430 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn         435 440 445 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr     450 455 460 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr 465 470 475 480 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln                 485 490 495 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys             500 505 510 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro         515 520 525 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys     530 535 540 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly 545 550 555 560 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr                 565 570 575 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr             580 585 590 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala         595 600 605 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu     610 615 620 Ser Leu Leu Arg 625 <210> 143 <211> 628 <212> PRT <213> Artificial Sequence <220> <223> HL185 STF2.R3.HA1-2 CA07 <400> 143 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Gly Val             180 185 190 Ala Pro Leu His Leu Gly Lys Cys Asn Ile Ala Gly Trp Ile Leu Gly         195 200 205 Asn Pro Glu Cys Glu Ser Leu Ser Thr Ala Ser Ser Trp Ser Tyr Ile     210 215 220 Val Glu Thr Pro Ser Ser Asp Asn Gly Thr Cys Tyr Pro Gly Asp Phe 225 230 235 240 Ile Asp Tyr Glu Glu Leu Arg Glu Gln Leu Ser Ser Val Ser Ser Phe                 245 250 255 Glu Arg Phe Glu Ile Phe Pro Lys Thr Ser Ser Trp Pro Asn His Asp             260 265 270 Ser Asn Lys Gly Val Thr Ala Ala Cys Pro His Ala Gly Ala Lys Ser         275 280 285 Phe Tyr Lys Asn Leu Ile Trp Leu Val Lys Lys Gly Asn Ser Tyr Pro     290 295 300 Lys Leu Ser Lys Ser Tyr Ile Asn Asp Lys Gly Lys Glu Val Leu Val 305 310 315 320 Leu Trp Gly Ile His His Pro Ser Thr Ser Ala Asp Gln Gln Ser Leu                 325 330 335 Tyr Gln Asn Ala Asp Ala Tyr Val Phe Val Gly Ser Ser Arg Tyr Ser             340 345 350 Lys Lys Phe Lys Pro Glu Ile Ala Ile Arg Pro Lys Val Arg Asp Gln         355 360 365 Glu Gly Arg Met Met Asn Tyr Tyr Trp Thr Leu Val Glu Pro Gly Asp Lys     370 375 380 Ile Thr Phe Glu Ala Thr Gly Asn Leu Val Val Pro Arg Tyr Ala Phe 385 390 395 400 Ala Met Glu Arg Asn Ala Gly Ser Gly Ile Ile Ser Ser Val Val                 405 410 415 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr             420 425 430 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn         435 440 445 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr     450 455 460 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr 465 470 475 480 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln                 485 490 495 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys             500 505 510 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro         515 520 525 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys     530 535 540 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly 545 550 555 560 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr                 565 570 575 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr             580 585 590 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala         595 600 605 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu     610 615 620 Ser Leu Leu Arg 625 <210> 144 <211> 628 <212> PRT <213> Artificial Sequence <220> <223> HL149 STF2.R3.HA1-2 IN5 <400> 144 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Gly Val             180 185 190 Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu Leu Gly         195 200 205 Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser Tyr Ile     210 215 220 Val Glu Lys Ala Asn Pro Thr Asn Asp Leu Cys Tyr Pro Gly Ser Phe 225 230 235 240 Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn His Phe                 245 250 255 Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His Glu Ala             260 265 270 Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Leu Gly Ser Pro Ser Phe         275 280 285 Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser Thr Tyr Pro Thr     290 295 300 Ile Lys Lys Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu Val Leu 305 310 315 320 Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Arg Leu Tyr                 325 330 335 Gln Asn Pro Thr Thr Tyr Ile Ser Ile Gly Thr Ser Thr Leu Asn Gln             340 345 350 Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Ser Val Val Asn Gly Gln Ser         355 360 365 Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp Ala Ile     370 375 380 Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala Tyr Lys 385 390 395 400 Ile Val Lys Lys Gly Asp Ser Ala Ile Met Lys Ser Glu Gly Val Val                 405 410 415 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr             420 425 430 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn         435 440 445 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr     450 455 460 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr 465 470 475 480 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln                 485 490 495 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys             500 505 510 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro         515 520 525 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys     530 535 540 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly 545 550 555 560 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr                 565 570 575 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr             580 585 590 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala         595 600 605 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu     610 615 620 Ser Leu Leu Arg 625 <210> 145 <211> 508 <212> PRT <213> Artificial Sequence <220> <223> HL199 STF2.R23.HA1-2 FL4 <400> 145 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr             180 185 190 Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro         195 200 205 Ser Ala Lys Ala Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly     210 215 220 Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn 225 230 235 240 Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile                 245 250 255 Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly             260 265 270 Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala         275 280 285 Trp Ala Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr     290 295 300 Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val 305 310 315 320 Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly                 325 330 335 Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr             340 345 350 His Tyr Val Ser Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly         355 360 365 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys     370 375 380 Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro 385 390 395 400 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly Lys                 405 410 415 Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val             420 425 430 Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser         435 440 445 Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg     450 455 460 Ser Arg Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser 465 470 475 480 Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala                 485 490 495 Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg             500 505 <210> 146 <211> 745 <212> PRT <213> Artificial Sequence <220> <223> HL077 STF2.HA1-2 FL4 <400> 146 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met 305 310 315 320 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu                 325 330 335 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly             340 345 350 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr         355 360 365 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val     370 375 380 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His 385 390 395 400 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr                 405 410 415 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala             420 425 430 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile         435 440 445 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg     450 455 460 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala 465 470 475 480 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln                 485 490 495 Val Pro Gln Asn Val Leu Ser Leu Leu Ala Gly Thr Arg Thr Arg Gly             500 505 510 Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu         515 520 525 Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile     530 535 540 Leu His Glu Val Lys Pro Val Thr Ser Gly Cys Phe Pro Ile Met His 545 550 555 560 Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu                 565 570 575 Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro             580 585 590 Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr         595 600 605 Ser Lys Ser Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp     610 615 620 Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile 625 630 635 640 Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp                 645 650 655 Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser Asn Pro Gln Lys             660 665 670 Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile         675 680 685 Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly     690 695 700 Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr 705 710 715 720 Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala                 725 730 735 Ser Gly Arg Ser Ser Val Valle Lys Gly             740 745 <210> 147 <211> 1292 <212> PRT <213> Artificial Sequence <220> <223> HL169 STF2.R3.HA1-2 B / BR60 <400> 147 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Lys Gly             180 185 190 Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp         195 200 205 Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser     210 215 220 Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys 225 230 235 240 Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu                 245 250 255 Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn             260 265 270 Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser         275 280 285 Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp     290 295 300 Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr 305 310 315 320 Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val                 325 330 335 Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly             340 345 350 Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr         355 360 365 His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly     370 375 380 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys 385 390 395 400 Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro                 405 410 415 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly Ser             420 425 430 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp         435 440 445 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp     450 455 460 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp 465 470 475 480 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala                 485 490 495 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala             500 505 510 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp         515 520 525 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala     530 535 540 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu 545 550 555 560 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp                 565 570 575 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly             580 585 590 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser         595 600 605 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln     610 615 620 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn 625 630 635 640 Val Leu Ser Leu Leu Arg Met Ala Gln Val Ile Asn Thr Asn Ser Leu                 645 650 655 Ser Leu Leu Thr Gln Asn Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly             660 665 670 Thr Ala Ile Glu Arg Leu Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys         675 680 685 Asp Asp Ala Ala Gly Ala Asn Arg Phe Thr Ala Asn Ile     690 695 700 Lys Gly Leu Thr Gln Ala Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile 705 710 715 720 Ala Gln Thr Thr Glu Gly Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln                 725 730 735 Arg Val Arg Glu Leu Ala Val Gln Ser Ala Asn Ser Thr Asn Ser Gln             740 745 750 Ser Asp Leu Asp Ser Ile Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu         755 760 765 Ile Asp Arg Val Ser Gly Gln Thr Gln Phe Asn Gly Val Lys Val Leu     770 775 780 Ala Gln Asp Asn Thr Leu Thr Ile Gln Val Gly Ala Asn Asp Gly Glu 785 790 795 800 Thr Ile Asp Ile Asp Leu Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu                 805 810 815 Asp Ser Leu Asn Val Gln Lys Ala Tyr Asp Val Lys Asp Thr Ala Val             820 825 830 Thr Thr Lys Ala Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys         835 840 845 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys     850 855 860 Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg 865 870 875 880 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 885 890 895 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser             900 905 910 Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys         915 920 925 Ile Gly Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe     930 935 940 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr 945 950 955 960 Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly                 965 970 975 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln             980 985 990 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser         995 1000 1005 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro     1010 1015 1020 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val 1025 1030 1035 1040 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln                 1045 1050 1055 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser             1060 1065 1070 Lys Val Ile Lys Gly Ser Val Val Ser Ala Asp Ala Lys Asn Ala Leu         1075 1080 1085 Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val     1090 1095 1100 Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr 1105 1110 1115 1120 Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala                 1125 1130 1135 Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly             1140 1145 1150 Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr         1155 1160 1165 Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala     1170 1175 1180 Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys 1185 1190 1195 1200 Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val                 1205 1210 1215 Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser             1220 1225 1230 Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg         1235 1240 1245 Ser Arg Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser     1250 1255 1260 Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala 1265 1270 1275 1280 Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 1285 1290 <210> 148 <211> 654 <212> PRT <213> Artificial Sequence <220> <223> HL483 STF2.R3.HA1-2 BR60 <400> 148 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Lys Gly             180 185 190 Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp         195 200 205 Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser     210 215 220 Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys 225 230 235 240 Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu                 245 250 255 Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn             260 265 270 Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser         275 280 285 Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp     290 295 300 Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr 305 310 315 320 Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val                 325 330 335 Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly             340 345 350 Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr         355 360 365 His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly     370 375 380 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys 385 390 395 400 Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro                 405 410 415 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly Ser             420 425 430 Leu Pro Leu Ile Gly Glu Ala Asp Val Val Ser Ala Asp Ala Lys Asn         435 440 445 Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu     450 455 460 Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly 465 470 475 480 Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp                 485 490 495 Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala             500 505 510 Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly         515 520 525 Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys     530 535 540 Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala 545 550 555 560 Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala                 565 570 575 Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe             580 585 590 Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu         595 600 605 Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn     610 615 620 Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala 625 630 635 640 Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 645 650 <210> 149 <211> 652 <212> PRT <213> Artificial Sequence <220> <223> HL610 STF2.R3.HA1-2 FL4 <400> 149 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Gly Thr             180 185 190 Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu         195 200 205 Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala     210 215 220 Lys Ala Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly Cys Phe 225 230 235 240 Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu                 245 250 255 Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala             260 265 270 Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys         275 280 285 Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala Trp Ala     290 295 300 Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr Val Glu 305 310 315 320 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly                 325 330 335 Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser             340 345 350 Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr         355 360 365 Val Ser Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu     370 375 380 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly 385 390 395 400 Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys                 405 410 415 Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Glu Gly Asp Leu Pro             420 425 430 Leu Asp Gly Glu Ala Asp Val Val Ser Ala Asp Ala Lys Asn Ala Leu         435 440 445 Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val     450 455 460 Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr 465 470 475 480 Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala                 485 490 495 Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly             500 505 510 Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr         515 520 525 Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala     530 535 540 Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys 545 550 555 560 Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val                 565 570 575 Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser             580 585 590 Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg         595 600 605 Ser Arg Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser     610 615 620 Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala 625 630 635 640 Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 645 650 <210> 150 <211> 654 <212> PRT <213> Artificial Sequence <220> <223> HL611 STF2.R3.HA1-2 BR60 <400> 150 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Glu Gly             180 185 190 Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp         195 200 205 Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser     210 215 220 Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys 225 230 235 240 Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu                 245 250 255 Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn             260 265 270 Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser         275 280 285 Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp     290 295 300 Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr 305 310 315 320 Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val                 325 330 335 Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly             340 345 350 Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr         355 360 365 His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly     370 375 380 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys 385 390 395 400 Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro                 405 410 415 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Val Glu Gly Asp             420 425 430 Leu Pro Leu Asp Gly Glu Ala Asp Val Val Ser Ala Asp Ala Lys Asn         435 440 445 Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu     450 455 460 Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly 465 470 475 480 Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp                 485 490 495 Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala             500 505 510 Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly         515 520 525 Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys     530 535 540 Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala 545 550 555 560 Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala                 565 570 575 Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe             580 585 590 Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu         595 600 605 Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn     610 615 620 Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala 625 630 635 640 Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 645 650 <210> 151 <211> 752 <212> PRT <213> Artificial Sequence <220> <223> HL656 STF2.D3Ins.HA1-2 FL4 D3I-o1 <400> 151 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys     290 295 300 Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Lys 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser             340 345 350 Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg         355 360 365 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Asn Lys Asn Ala 385 390 395 400 Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu                 405 410 415 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met             420 425 430 Lys Asn Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala         435 440 445 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Ser Phe Pro Asp     450 455 460 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp 465 470 475 480 Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg                 485 490 495 Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser             500 505 510 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys Thr         515 520 525 Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala     530 535 540 Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly 545 550 555 560 Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile                 565 570 575 Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp             580 585 590 Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr         595 600 605 Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val     610 615 620 Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala 625 630 635 640 Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu                 645 650 655 Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala             660 665 670 Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn         675 680 685 Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu     690 695 700 Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val 705 710 715 720 Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val                 725 730 735 Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg             740 745 750 <210> 152 <211> 652 <212> PRT <213> Artificial Sequence <220> <223> HL724 STF2.R3.HA1-2 WI1 <400> 152 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Gly Thr             180 185 190 Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu         195 200 205 Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala     210 215 220 Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe 225 230 235 240 Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu                 245 250 255 Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala             260 265 270 Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys         275 280 285 Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala     290 295 300 Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu 305 310 315 320 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly                 325 330 335 Phe His Ser Asp Asn Lys Thr Gln Met Lys Ser Leu Tyr Gly Asp Ser             340 345 350 Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr         355 360 365 Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu     370 375 380 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly 385 390 395 400 Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys                 405 410 415 Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Glu Gly Asp Leu Pro             420 425 430 Leu Asp Gly Glu Ala Asp Val Val Ser Ala Asp Ala Lys Asn Ala Leu         435 440 445 Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val     450 455 460 Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr 465 470 475 480 Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala                 485 490 495 Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly             500 505 510 Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr         515 520 525 Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala     530 535 540 Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys 545 550 555 560 Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val                 565 570 575 Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser             580 585 590 Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg         595 600 605 Ser Arg Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser     610 615 620 Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala 625 630 635 640 Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 645 650 <210> 153 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Peptide for HA1-2 modified C-terminus <400> 153 Glu Gly Asp Leu Pro Leu Asp Gly Glu Ala Asp  1 5 10 <210> 154 <211> 652 <212> PRT <213> Artificial Sequence <220> <223> HL719 STF2.R3.HA1-2 WI1 <400> 154 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Gly Thr             180 185 190 Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu         195 200 205 Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala     210 215 220 Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe 225 230 235 240 Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu                 245 250 255 Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala             260 265 270 Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys         275 280 285 Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala     290 295 300 Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu 305 310 315 320 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly                 325 330 335 Phe His Ser Asp Asn Lys Thr Gln Met Lys Ser Leu Tyr Gly Asp Ser             340 345 350 Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr         355 360 365 Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu     370 375 380 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly 385 390 395 400 Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys                 405 410 415 Val Trp Cys Ala Ser Gly Arg Ser Ser Lys Val Ile Lys Gly Ser Leu Pro             420 425 430 Leu Ile Gly Glu Ala Asp Val Val Ser Ala Asp Ala Lys Asn Ala Leu         435 440 445 Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val     450 455 460 Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr 465 470 475 480 Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala                 485 490 495 Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly             500 505 510 Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr         515 520 525 Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala     530 535 540 Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys 545 550 555 560 Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val                 565 570 575 Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser             580 585 590 Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg         595 600 605 Ser Arg Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser     610 615 620 Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala 625 630 635 640 Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 645 650 <210> 155 <211> 654 <212> PRT <213> Artificial Sequence <220> <223> HL753 STF2.R3.HA1-2 HK259 <400> 155 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Lys Gly             180 185 190 Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Pro Asn Cys Thr Asp         195 200 205 Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser     210 215 220 Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys 225 230 235 240 Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu                 245 250 255 Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn             260 265 270 Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser         275 280 285 Cys Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp     290 295 300 Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr 305 310 315 320 Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val                 325 330 335 Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly             340 345 350 Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr         355 360 365 His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly     370 375 380 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys 385 390 395 400 Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro                 405 410 415 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Val Glu Gly Asp             420 425 430 Leu Pro Leu Asp Gly Glu Ala Asp Val Val Ser Ala Asp Ala Lys Asn         435 440 445 Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu     450 455 460 Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly 465 470 475 480 Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp                 485 490 495 Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala             500 505 510 Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly         515 520 525 Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys     530 535 540 Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala 545 550 555 560 Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala                 565 570 575 Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe             580 585 590 Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu         595 600 605 Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn     610 615 620 Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala 625 630 635 640 Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 645 650 <210> 156 <211> 653 <212> PRT <213> Artificial Sequence <220> <223> HL742 STF2.R3.HA1-2 BD5495 <400> 156 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Gly Thr             180 185 190 Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu         195 200 205 Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser Ala     210 215 220 Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe 225 230 235 240 Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu                 245 250 255 Arg Gly Tyr Glu His Ile Arg Leu Ser Thr Asn Asn Val Ile Asn Ala             260 265 270 Gly Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys         275 280 285 Pro Asn Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala     290 295 300 Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr Ile 305 310 315 320 Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp                 325 330 335 Gly Phe His Ser Asp Asn Glu Ile Gln Met Ala Lys Leu Tyr Gly Asp             340 345 350 Ser Arg Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His         355 360 365 Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly     370 375 380 Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser 385 390 395 400 Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln                 405 410 415 Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Val Glu Gly Asp Leu             420 425 430 Pro Leu Asp Gly Glu Ala Asp Val Val Ser Ala Asp Ala Lys Asn Ala         435 440 445 Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu     450 455 460 Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly 465 470 475 480 Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu                 485 490 495 Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp             500 505 510 Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys         515 520 525 Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala     530 535 540 Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala 545 550 555 560 Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln                 565 570 575 Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn             580 585 590 Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala         595 600 605 Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met     610 615 620 Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln 625 630 635 640 Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 645 650 <210> 157 <211> 753 <212> PRT <213> Artificial Sequence <220> <223> HL774 STF2.D3Ins.HA1-2 HK259 D3I-o1 <400> 157 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys         275 280 285 Cys Pro Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys     290 295 300 Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser             340 345 350 Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys         355 360 365 Ile Gly Thr Ser Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr 385 390 395 400 Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly                 405 410 415 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln             420 425 430 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser         435 440 445 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro     450 455 460 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val 465 470 475 480 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln                 485 490 495 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser             500 505 510 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys         515 520 525 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp     530 535 540 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn 545 550 555 560 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr                 565 570 575 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala             580 585 590 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr         595 600 605 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly     610 615 620 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn 625 630 635 640 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala                 645 650 655 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala             660 665 670 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln         675 680 685 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn     690 695 700 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu 705 710 715 720 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser                 725 730 735 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu             740 745 750 Arg      <210> 158 <211> 753 <212> PRT <213> Artificial Sequence <220> <223> HL787 STF2.D3Ins.HA1-2 BD5495 D3I-o1 <400> 158 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys     290 295 300 Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser             340 345 350 Thr Asn Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys         355 360 365 Ile Gly Thr Ser Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr 385 390 395 400 Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly                 405 410 415 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Ile Gln             420 425 430 Met Ala Lys Leu Tyr Gly Asp Ser Arg Pro Gln Lys Phe Thr Ser Ser         435 440 445 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro     450 455 460 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val 465 470 475 480 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln                 485 490 495 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser             500 505 510 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys         515 520 525 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp     530 535 540 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn 545 550 555 560 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr                 565 570 575 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala             580 585 590 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr         595 600 605 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly     610 615 620 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn 625 630 635 640 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala                 645 650 655 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala             660 665 670 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln         675 680 685 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn     690 695 700 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu 705 710 715 720 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser                 725 730 735 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu             740 745 750 Arg      <210> 159 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL849 STF2.D3Ins.HA1-2 WI1 D3I-i1 <400> 159 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys             260 265 270 Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val         275 280 285 Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro     290 295 300 Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg 305 310 315 320 Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr                 325 330 335 Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu             340 345 350 Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe         355 360 365 Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr     370 375 380 Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp 385 390 395 400 Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met Lys                 405 410 415 Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn             420 425 430 Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp Gln         435 440 445 Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr     450 455 460 Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly 465 470 475 480 Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val                 485 490 495 Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Asp Gly Thr Val             500 505 510 Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala Thr         515 520 525 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser     530 535 540 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp 545 550 555 560 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly                 565 570 575 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr             580 585 590 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr         595 600 605 Ser Tyr Thr Ala Asp Asp Gly Thr     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 160 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL848 STF2.D3Ins.HA1-2 WI1 D3I-s1 <400> 160 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp                 245 250 255 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys             260 265 270 Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg         275 280 285 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile     290 295 300 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser 305 310 315 320 Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg                 325 330 335 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe             340 345 350 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala         355 360 365 Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu     370 375 380 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met 385 390 395 400 Lys Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala                 405 410 415 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp             420 425 430 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp         435 440 445 Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg     450 455 460 Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser 465 470 475 480 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Ala Asp Ala                 485 490 495 Ala Lys Asn Gly Asp Tyr Glu Val Asn Val Ala Thr Asp Gly Thr Val             500 505 510 Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala Thr         515 520 525 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser     530 535 540 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp 545 550 555 560 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly                 565 570 575 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr             580 585 590 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr         595 600 605 Ser Tyr Thr Ala Asp Asp Gly Thr     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 161 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL825 STF2.D2Ins.HA1-2 WI1 D2I-o1 <400> 161 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Lys Gly Thr Arg Thr             180 185 190 Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val         195 200 205 Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala     210 215 220 Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile 225 230 235 240 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly                 245 250 255 Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys             260 265 270 Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn         275 280 285 Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro     290 295 300 Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro 305 310 315 320 Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His                 325 330 335 Ser Asp Asn Lys Thr Gln Met Lys Ser Leu Tyr Gly Asp Ser Asn Pro             340 345 350 Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser         355 360 365 Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln     370 375 380 Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr 385 390 395 400 Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp                 405 410 415 Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile             420 425 430 Gly Glu Ala Asp Thr Lys Ala Tyr Ala Asn Asn Gly Thr Thr Leu Asp         435 440 445 Val Ser Gly Leu Asp Asp Ala Ile Lys Ala Ala Thr Gly Gly Thr     450 455 460 Asn Gly Thr Ala Ser Val Thr Gly Gly Ala Val Lys Phe Asp Ala Asp 465 470 475 480 Asn Asn Lys Tyr Phe Val Thr Ile Gly Gly Phe Thr Gly Ala Asp Ala                 485 490 495 Ala Lys Asn Gly Asp Tyr Glu Val Asn Val Ala Thr Asp Gly Thr Val             500 505 510 Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala Thr         515 520 525 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser     530 535 540 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp 545 550 555 560 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly                 565 570 575 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr             580 585 590 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr         595 600 605 Ser Tyr Thr Ala Asp Asp Gly Thr     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 162 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL826 STF2.D2Ins.HA1-2 WI1 D2I-o2 <400> 162 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu             180 185 190 Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly         195 200 205 Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val     210 215 220 Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln 225 230 235 240 Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln                 245 250 255 Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly             260 265 270 Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala         275 280 285 Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn     290 295 300 Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln 305 310 315 320 Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met Lys Ser                 325 330 335 Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly             340 345 350 Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr         355 360 365 Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met     370 375 380 Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val 385 390 395 400 Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Lys Val Ile                 405 410 415 Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Tyr Asp Val Lys Asp             420 425 430 Thr Ala Val Thr Thr Lys Ala Tyr Ala Asn Asn Gly Thr Thr Leu Asp         435 440 445 Val Ser Gly Leu Asp Asp Ala Ile Lys Ala Ala Thr Gly Gly Thr     450 455 460 Asn Gly Thr Ala Ser Val Thr Gly Gly Ala Val Lys Phe Asp Ala Asp 465 470 475 480 Asn Asn Lys Tyr Phe Val Thr Ile Gly Gly Phe Thr Gly Ala Asp Ala                 485 490 495 Ala Lys Asn Gly Asp Tyr Glu Val Asn Val Ala Thr Asp Gly Thr Val             500 505 510 Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala Thr         515 520 525 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser     530 535 540 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp 545 550 555 560 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly                 565 570 575 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr             580 585 590 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr         595 600 605 Ser Tyr Thr Ala Asp Asp Gly Thr     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 163 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL827 STF2.D2Ins.HA1-2 WI1 D2I-o3 <400> 163 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met 305 310 315 320 Ser Tyr Thr Asp Lys Asn Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys                 325 330 335 Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro             340 345 350 Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu         355 360 365 Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr     370 375 380 Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg 385 390 395 400 Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro                 405 410 415 Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile             420 425 430 Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys         435 440 445 Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu     450 455 460 Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr 465 470 475 480 Gln Met Lys Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser                 485 490 495 Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe             500 505 510 Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val         515 520 525 Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr     530 535 540 Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg 545 550 555 560 Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Gly                 565 570 575 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr             580 585 590 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr         595 600 605 Ser Tyr Thr Ala Asp Asp Gly Thr     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 164 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL828 STF2.D1Ins.HA1-2 WI1 D1I-o1 <400> 164 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys             100 105 110 Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro         115 120 125 Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu     130 135 140 Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr 145 150 155 160 Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg                 165 170 175 Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro             180 185 190 Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile         195 200 205 Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys     210 215 220 Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu 225 230 235 240 Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr                 245 250 255 Gln Met Lys Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser             260 265 270 Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe         275 280 285 Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val     290 295 300 Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr 305 310 315 320 Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg                 325 330 335 Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr             340 345 350 Asn Ser Gln Ser Asp Leu Asp Ser Ile Gln Ala Glu Ile Thr Gln Arg         355 360 365 Leu Asn Glu Ile Asp Arg Val Ser Gly Gln Thr Gln Phe Asn Gly Val     370 375 380 Lys Val Leu Ala Gln Asp Asn Thr Leu Thr Ile Gln Val Gly Ala Asn 385 390 395 400 Asp Gly Glu Thr Ile Asp Ile Asp Leu Lys Gln Ile Asn Ser Gln Thr                 405 410 415 Leu Gly Leu Asp Ser Leu Asn Val Gln Lys Ala Tyr Asp Val Lys Asp             420 425 430 Thr Ala Val Thr Thr Lys Ala Tyr Ala Asn Asn Gly Thr Thr Leu Asp         435 440 445 Val Ser Gly Leu Asp Asp Ala Ile Lys Ala Ala Thr Gly Gly Thr     450 455 460 Asn Gly Thr Ala Ser Val Thr Gly Gly Ala Val Lys Phe Asp Ala Asp 465 470 475 480 Asn Asn Lys Tyr Phe Val Thr Ile Gly Gly Phe Thr Gly Ala Asp Ala                 485 490 495 Ala Lys Asn Gly Asp Tyr Glu Val Asn Val Ala Thr Asp Gly Thr Val             500 505 510 Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala Thr         515 520 525 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser     530 535 540 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp 545 550 555 560 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly                 565 570 575 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr             580 585 590 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr         595 600 605 Ser Tyr Thr Ala Asp Asp Gly Thr     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 165 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL850 STF2.D2Ins.HA1-2 WI1 D2I-i1 <400> 165 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met 305 310 315 320 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu                 325 330 335 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly             340 345 350 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Lys Gly         355 360 365 Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp     370 375 380 Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser 385 390 395 400 Ala Lys Ala Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys                 405 410 415 Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu             420 425 430 Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp         435 440 445 Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser     450 455 460 Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp 465 470 475 480 Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val                 485 490 495 Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp             500 505 510 Gly Phe His Ser Asp Asn Lys Thr Gln Met Lys Ser Leu Tyr Gly Asp         515 520 525 Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His     530 535 540 Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly 545 550 555 560 Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro                 565 570 575 Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln             580 585 590 Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly Ser Leu         595 600 605 Pro Leu Ile Gly Glu Ala Asp Thr Thr Lys Thr Ala Ala Asn Gln Leu     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 166 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL733 STF2.D2Ins.HA1-2 BR60 D2I-o1 <400> 166 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Gly Lys Gly Thr Glu Thr             180 185 190 Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp Val         195 200 205 Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg Val     210 215 220 Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile 225 230 235 240 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly                 245 250 255 Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn Ala Glu Asn             260 265 270 Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro Asn         275 280 285 Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro     290 295 300 Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu Val 305 310 315 320 Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe                 325 330 335 His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser Lys             340 345 350 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val         355 360 365 Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu Pro     370 375 380 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly Lys 385 390 395 400 Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys Val                 405 410 415 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu             420 425 430 Ile Gly Aly Asp Gly Aly Asp Gly Aly Asn Gly Thr Thr Leu         435 440 445 Asp Val Ser Gly Leu Asp Asp Ala Ala Ile Lys Ala Ala Thr Gly Gly     450 455 460 Thr Asn Gly Thr Ala Ser Val Thr Gly Gly Ala Val Lys Phe Asp Ala 465 470 475 480 Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly Gly Phe Thr Gly Ala Asp                 485 490 495 Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn Ala Thr Asp Gly Thr             500 505 510 Val Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala         515 520 525 Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val     530 535 540 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr 545 550 555 560 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn                 565 570 575 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr             580 585 590 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr         595 600 605 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln     610 615 620 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 167 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL856 STF2.D2Ins.HA1-2 BR60 D2I-o1 <400> 167 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Lys Gly Thr Glu Thr             180 185 190 Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp Val         195 200 205 Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg Val     210 215 220 Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile 225 230 235 240 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly                 245 250 255 Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn Ala Glu Asn             260 265 270 Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro Asn         275 280 285 Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro     290 295 300 Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu Val 305 310 315 320 Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe                 325 330 335 His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser Lys             340 345 350 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val         355 360 365 Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu Pro     370 375 380 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly Lys 385 390 395 400 Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys Val                 405 410 415 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu             420 425 430 Ile Gly Glu Ala Asp Thr Lys Ala Tyr Ala Asn Gly Thr Thr Leu         435 440 445 Asp Val Ser Gly Leu Asp Asp Ala Ala Ile Lys Ala Ala Thr Gly Gly     450 455 460 Thr Asn Gly Thr Ala Ser Val Thr Gly Gly Ala Val Lys Phe Asp Ala 465 470 475 480 Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly Gly Phe Thr Gly Ala Asp                 485 490 495 Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn Ala Thr Asp Gly Thr             500 505 510 Val Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala         515 520 525 Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val     530 535 540 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr 545 550 555 560 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn                 565 570 575 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr             580 585 590 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr         595 600 605 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln     610 615 620 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 168 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL857 STF2.D2Ins.HA1-2 BR60 D2I-o2 <400> 168 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu             180 185 190 Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly         195 200 205 Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val     210 215 220 Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln 225 230 235 240 Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His                 245 250 255 Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly             260 265 270 Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala         275 280 285 Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr     290 295 300 Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp 305 310 315 320 Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala                 325 330 335 Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn             340 345 350 Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln         355 360 365 Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr     370 375 380 Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly 385 390 395 400 Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Val                 405 410 415 Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Tyr Asp Val Lys             420 425 430 Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala Asn Asn Gly Thr Thr Leu         435 440 445 Asp Val Ser Gly Leu Asp Asp Ala Ala Ile Lys Ala Ala Thr Gly Gly     450 455 460 Thr Asn Gly Thr Ala Ser Val Thr Gly Gly Ala Val Lys Phe Asp Ala 465 470 475 480 Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly Gly Phe Thr Gly Ala Asp                 485 490 495 Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn Ala Thr Asp Gly Thr             500 505 510 Val Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala         515 520 525 Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val     530 535 540 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr 545 550 555 560 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn                 565 570 575 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr             580 585 590 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr         595 600 605 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln     610 615 620 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 169 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL888 STF2.D3Ins.HA1-2 WI1 D3I-o2 <400> 169 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys 225 230 235 240 Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro                 245 250 255 Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu             260 265 270 Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr         275 280 285 Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg     290 295 300 Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro 305 310 315 320 Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile                 325 330 335 Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys             340 345 350 Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu         355 360 365 Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr     370 375 380 Gln Met Lys Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser 385 390 395 400 Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe                 405 410 415 Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val             420 425 430 Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr         435 440 445 Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg     450 455 460 Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Asp 465 470 475 480 Asn Asn Lys Tyr Phe Val Thr Ile Gly Gly Phe Thr Gly Ala Asp Ala                 485 490 495 Ala Lys Asn Gly Asp Tyr Glu Val Asn Val Ala Thr Asp Gly Thr Val             500 505 510 Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala Thr         515 520 525 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser     530 535 540 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp 545 550 555 560 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly                 565 570 575 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr             580 585 590 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr         595 600 605 Ser Tyr Thr Ala Asp Asp Gly Thr     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 170 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL890 STF2.D3Ins.HA1-2 WI1 D2I-c1 <400> 170 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp 305 310 315 320 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys                 325 330 335 Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg             340 345 350 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile         355 360 365 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser     370 375 380 Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg 385 390 395 400 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe                 405 410 415 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala             420 425 430 Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu         435 440 445 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met     450 455 460 Lys Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala 465 470 475 480 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp                 485 490 495 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp             500 505 510 Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg         515 520 525 Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser     530 535 540 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Ala Thr Asp 545 550 555 560 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly                 565 570 575 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr             580 585 590 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr         595 600 605 Ser Tyr Thr Ala Asp Asp Gly Thr     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 171 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL892 STF2.D2Ins.HA1-2 WI1 D2I-i2 <400> 171 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met 305 310 315 320 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu                 325 330 335 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly             340 345 350 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr         355 360 365 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val     370 375 380 Val Thr Ile Asp Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp 385 390 395 400 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys                 405 410 415 Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg             420 425 430 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile         435 440 445 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser     450 455 460 Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg 465 470 475 480 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe                 485 490 495 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala             500 505 510 Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu         515 520 525 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met     530 535 540 Lys Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala 545 550 555 560 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp                 565 570 575 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp             580 585 590 Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg         595 600 605 Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser     610 615 620 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 172 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL858 STF2.D3Ins.HA1-2 BR60 D2I-o3 <400> 172 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met 305 310 315 320 Ser Tyr Thr Asp Lys Asn Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys                 325 330 335 Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro             340 345 350 Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu         355 360 365 Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr     370 375 380 Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg 385 390 395 400 Leu Ser Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro                 405 410 415 Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn             420 425 430 Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn         435 440 445 Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr     450 455 460 Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu 465 470 475 480 Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr                 485 490 495 Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly             500 505 510 Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile         515 520 525 Val Val Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr     530 535 540 Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly 545 550 555 560 Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp                 565 570 575 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr             580 585 590 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr         595 600 605 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln     610 615 620 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 173 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL860 STF2.D3Ins.HA1-2 BR60 D3I-s1 <400> 173 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys                 245 250 255 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys             260 265 270 Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg         275 280 285 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile     290 295 300 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser 305 310 315 320 Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys                 325 330 335 Ile Gly Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe             340 345 350 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr         355 360 365 Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly     370 375 380 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln 385 390 395 400 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser                 405 410 415 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro             420 425 430 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val         435 440 445 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln     450 455 460 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser 465 470 475 480 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Ala Asp                 485 490 495 Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn Ala Thr Asp Gly Thr             500 505 510 Val Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala         515 520 525 Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val     530 535 540 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr 545 550 555 560 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn                 565 570 575 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr             580 585 590 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr         595 600 605 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln     610 615 620 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 174 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL889 STF2.D3Ins.HA1-2 BR60 D3I-o2 <400> 174 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys 225 230 235 240 Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro                 245 250 255 Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu             260 265 270 Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr         275 280 285 Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg     290 295 300 Leu Ser Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro 305 310 315 320 Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn                 325 330 335 Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn             340 345 350 Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr         355 360 365 Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu     370 375 380 Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr 385 390 395 400 Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly                 405 410 415 Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile             420 425 430 Val Val Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr         435 440 445 Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly     450 455 460 Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp 465 470 475 480 Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly Gly Phe Thr Gly Ala Asp                 485 490 495 Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn Ala Thr Asp Gly Thr             500 505 510 Val Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala         515 520 525 Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val     530 535 540 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr 545 550 555 560 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn                 565 570 575 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr             580 585 590 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr         595 600 605 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln     610 615 620 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 175 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL891 STF2.D2Ins.HA1-2 BR60 D2I-c1 <400> 175 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys 305 310 315 320 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys                 325 330 335 Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg             340 345 350 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile         355 360 365 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser     370 375 380 Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys 385 390 395 400 Ile Gly Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe                 405 410 415 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr             420 425 430 Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly         435 440 445 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln     450 455 460 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser 465 470 475 480 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro                 485 490 495 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val             500 505 510 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln         515 520 525 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser     530 535 540 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Ala Thr 545 550 555 560 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn                 565 570 575 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr             580 585 590 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr         595 600 605 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln     610 615 620 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 176 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL893 STF2.D2Ins.HA1-2 BR60 D2I-i2 <400> 176 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met 305 310 315 320 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu                 325 330 335 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly             340 345 350 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr         355 360 365 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val     370 375 380 Val Thr Ile Asp Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys 385 390 395 400 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys                 405 410 415 Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg             420 425 430 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile         435 440 445 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser     450 455 460 Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys 465 470 475 480 Ile Gly Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe                 485 490 495 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr             500 505 510 Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly         515 520 525 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln     530 535 540 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser 545 550 555 560 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro                 565 570 575 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val             580 585 590 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln         595 600 605 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser     610 615 620 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 177 <211> 752 <212> PRT <213> Artificial Sequence <220> <223> HL864 STF2.D3Ins.HA1-2 WI1 mutations <400> 177 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Lys Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys     290 295 300 Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser             340 345 350 Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg         355 360 365 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala 385 390 395 400 Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu                 405 410 415 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met             420 425 430 Lys Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala         435 440 445 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp     450 455 460 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp 465 470 475 480 Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg                 485 490 495 Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser             500 505 510 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys Thr         515 520 525 Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala     530 535 540 Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly 545 550 555 560 Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile                 565 570 575 Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp             580 585 590 Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr         595 600 605 Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val     610 615 620 Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala 625 630 635 640 Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu                 645 650 655 Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala             660 665 670 Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn         675 680 685 Arg Phe Asn Val Ala Ile Thr Val Leu Gly Asn Thr Val Asn Asn Leu     690 695 700 Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val 705 710 715 720 Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val                 725 730 735 Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg             740 745 750 <210> 178 <211> 503 <212> PRT <213> Artificial Sequence <220> <223> Flagellin (FljB) with mutations <400> 178 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Lys Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro         275 280 285 Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val     290 295 300 Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr 305 310 315 320 Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly                 325 330 335 Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys             340 345 350 Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala         355 360 365 Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile     370 375 380 Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys 385 390 395 400 Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro                 405 410 415 Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser             420 425 430 Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Val Ala Ile Thr Val Leu         435 440 445 Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp     450 455 460 Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu 465 470 475 480 Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln                 485 490 495 Asn Val Leu Ser Leu Leu Arg             500 <210> 179 <211> 654 <212> PRT <213> Artificial Sequence <220> <223> HL854 STF2.D2Ins.HA1-2 B / WI1, no D3 <400> 179 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Gly Lys Gly Thr Arg Thr             180 185 190 Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val         195 200 205 Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala     210 215 220 Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile 225 230 235 240 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly                 245 250 255 Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys             260 265 270 Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn         275 280 285 Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro     290 295 300 Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro 305 310 315 320 Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His                 325 330 335 Ser Asp Asn Lys Thr Gln Met Lys Ser Leu Tyr Gly Asp Ser Asn Pro             340 345 350 Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser         355 360 365 Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln     370 375 380 Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr 385 390 395 400 Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp                 405 410 415 Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile             420 425 430 Gly Glu Ala Asp Aly Lys Asn Ala Val Val Ser Ala Asp Ala Lys Asn         435 440 445 Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu     450 455 460 Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly 465 470 475 480 Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp                 485 490 495 Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala             500 505 510 Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly         515 520 525 Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys     530 535 540 Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala 545 550 555 560 Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala                 565 570 575 Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe             580 585 590 Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu         595 600 605 Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn     610 615 620 Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala 625 630 635 640 Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg                 645 650 <210> 180 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL 861 STF2.D3Ins.HA1-2 BR60 D3I-i1 <400> 180 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys             260 265 270 Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr         275 280 285 Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg Pro     290 295 300 Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg 305 310 315 320 Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr                 325 330 335 His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile             340 345 350 Gly Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe         355 360 365 Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala     370 375 380 Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu 385 390 395 400 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met                 405 410 415 Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala             420 425 430 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn         435 440 445 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp     450 455 460 Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg 465 470 475 480 Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser                 485 490 495 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Asp Gly Thr             500 505 510 Val Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala         515 520 525 Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val     530 535 540 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr 545 550 555 560 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn                 565 570 575 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr             580 585 590 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr         595 600 605 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln     610 615 620 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 181 <211> 756 <212> PRT <213> Artificial Sequence <220> <223> HL862 STF2.D2Ins.HA1-2 BR60 D2I-i1 <400> 181 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met 305 310 315 320 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu                 325 330 335 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly             340 345 350 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Lys Gly         355 360 365 Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp     370 375 380 Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser 385 390 395 400 Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys                 405 410 415 Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu             420 425 430 Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn         435 440 445 Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser     450 455 460 Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp 465 470 475 480 Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr                 485 490 495 Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val             500 505 510 Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly         515 520 525 Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr     530 535 540 His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly 545 550 555 560 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys                 565 570 575 Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro             580 585 590 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly Ser         595 600 605 Leu Pro Leu Ile Gly Glu Ala Asp Thr Thr Lys Thr Ala Ala Asn Gln     610 615 620 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys 625 630 635 640 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro                 645 650 655 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys             660 665 670 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly         675 680 685 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr     690 695 700 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr 705 710 715 720 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala                 725 730 735 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu             740 745 750 Ser Leu Leu Arg         755 <210> 182 <211> 752 <212> PRT <213> Artificial Sequence <220> <223> HL863 STF2.D3Ins.HA1-2 SI379 D3I-o1 <400> 182 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Thr         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys     290 295 300 Val Gly Ile Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Ile Lys 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Lys Ile Arg Leu Ser             340 345 350 Thr Gln Asn Val Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg         355 360 365 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Arg Asp Asn Asn Lys Thr Ala 385 390 395 400 Thr Asn Pro Leu Thr Val Glu Val Pro His Ile Cys Thr Lys Glu Glu                 405 410 415 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met             420 425 430 Lys Asn Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala         435 440 445 Asn Gly Ile Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asp     450 455 460 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp 465 470 475 480 Tyr Met Val Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg                 485 490 495 Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser             500 505 510 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys Thr         515 520 525 Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala     530 535 540 Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly 545 550 555 560 Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile                 565 570 575 Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp             580 585 590 Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr         595 600 605 Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val     610 615 620 Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala 625 630 635 640 Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu                 645 650 655 Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala             660 665 670 Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn         675 680 685 Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu     690 695 700 Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val 705 710 715 720 Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val                 725 730 735 Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg             740 745 750 <210> 183 <211> 755 <212> PRT <213> Artificial Sequence <220> <223> HL903 STF2.D3Ins.HA1-2 SI379 D3I-i1 <400> 183 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Thr Cys             260 265 270 Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val         275 280 285 Gly Ile Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Ile Lys Pro     290 295 300 Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg 305 310 315 320 Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Lys Ile Arg Leu Ser Thr                 325 330 335 Gln Asn Val Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu             340 345 350 Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe         355 360 365 Ala Thr Met Ala Trp Ala Val Pro Arg Asp Asn Asn Lys Thr Ala Thr     370 375 380 Asn Pro Leu Thr Val Glu Val Pro His Ile Cys Thr Lys Glu Glu Asp 385 390 395 400 Gln Ile Thr Val Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys                 405 410 415 Asn Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn             420 425 430 Gly Ile Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asp Gln         435 440 445 Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr     450 455 460 Met Val Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly 465 470 475 480 Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Val                 485 490 495 Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Asp Gly Thr Val             500 505 510 Thr Leu Ala Ala Gly Ala Thr Lys Thr Thr Met Pro Ala Gly Ala Thr         515 520 525 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser     530 535 540 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp 545 550 555 560 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly                 565 570 575 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr             580 585 590 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr         595 600 605 Ser Tyr Thr Ala Asp Asp Gly Thr     610 615 620 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr 625 630 635 640 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu                 645 650 655 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile             660 665 670 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala         675 680 685 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val     690 695 700 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala 705 710 715 720 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly                 725 730 735 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser             740 745 750 Leu Leu Arg         755 <210> 184 <211> 752 <212> PRT <213> Artificial Sequence <220> <223> HL869 STF2.D3Ins.HA1-2 HU158 D3I-o1 <400> 184 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys     290 295 300 Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser             340 345 350 Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg         355 360 365 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala 385 390 395 400 Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu                 405 410 415 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Asn Gln Met             420 425 430 Lys Ser Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala         435 440 445 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp     450 455 460 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp 465 470 475 480 Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg                 485 490 495 Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser             500 505 510 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys Thr         515 520 525 Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala     530 535 540 Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly 545 550 555 560 Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile                 565 570 575 Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp             580 585 590 Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr         595 600 605 Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val     610 615 620 Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala 625 630 635 640 Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu                 645 650 655 Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala             660 665 670 Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn         675 680 685 Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu     690 695 700 Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val 705 710 715 720 Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val                 725 730 735 Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg             740 745 750 <210> 185 <211> 752 <212> PRT <213> Artificial Sequence <220> <223> HL871 STF2.D3Ins.HA1-2 TX6 D3I-o1 <400> 185 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys     290 295 300 Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser             340 345 350 Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg         355 360 365 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ile Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Tyr Lys Asn Ala 385 390 395 400 Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Lys Glu Glu Glu                 405 410 415 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Lys Thr Gln Met             420 425 430 Lys Asn Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala         435 440 445 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Asp Phe Pro Asp     450 455 460 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp 465 470 475 480 Tyr Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg                 485 490 495 Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser             500 505 510 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys Thr         515 520 525 Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala     530 535 540 Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly 545 550 555 560 Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile                 565 570 575 Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp             580 585 590 Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr         595 600 605 Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val     610 615 620 Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala 625 630 635 640 Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu                 645 650 655 Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala             660 665 670 Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn         675 680 685 Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu     690 695 700 Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val 705 710 715 720 Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val                 725 730 735 Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg             740 745 750 <210> 186 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> HL639 STF2.D3Ins.HA1-L DE16 D3I-o1 <400> 186 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Glu Ile Cys         275 280 285 Asp Ser Pro His Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp 305 310 315 320 Asp Leu Phe Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln         355 360 365 Asn Gly Thr Ser Ser Ala Cys Ile Arg Ser Ser Lys Asn Ser Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr His Leu Asn Phe Lys Tyr Pro Ala Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Ile Trp                 405 410 415 Gly Val His His Pro Gly Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala             420 425 430 Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr         435 440 445 Val Ser Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu 465 470 475 480 Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile                 485 490 495 Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys             500 505 510 Cys Asn Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr     530 535 540 Val Lys Gln Asn Thr Leu Lys Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 187 <211> 680 <212> PRT <213> Artificial Sequence <220> <223> HL836 STF2.D3Ins.HA1-L VT361 D3I-o1 <400> 187 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Glu Leu             180 185 190 Val Gln Asn Ser Ser Ile Gly Glu Ile Cys Asp Ser Pro His Gln Ile         195 200 205 Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly Asp Pro     210 215 220 Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe Val Glu Arg 225 230 235 240 Ser Lys Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp Tyr Ala                 245 250 255 Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe Asn Asn             260 265 270 Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser Ser Ala         275 280 285 Cys Ile Arg Arg Ser Asn Asn Ser Phe Phe Ser Arg Leu Asn Trp Leu     290 295 300 Thr Gln Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr Met Pro Asn 305 310 315 320 Asn Glu Gln Phe Asp Lys Leu Tyr Ile Trp Gly Val His His Pro Val                 325 330 335 Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ser Ser Gly Arg Ile             340 345 350 Thr Val Ser Thr Lys Arg Ser Gln Gln Ala Val Ile Pro Asn Ile Gly         355 360 365 Tyr Arg Pro Arg Ile Arg Asn Ile Pro Ser Arg Ile Ser Ile Tyr Trp     370 375 380 Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr Gly Asn 385 390 395 400 Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys Ser Ser                 405 410 415 Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu Cys Ile             420 425 430 Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn Val Asn         435 440 445 Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Ser Thr Leu     450 455 460 Lys Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly 465 470 475 480 Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr                 485 490 495 Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala             500 505 510 Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile         515 520 525 Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr     530 535 540 Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr 545 550 555 560 Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe                 565 570 575 Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn             580 585 590 Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg         595 600 605 Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn     610 615 620 Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu 625 630 635 640 Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile                 645 650 655 Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro             660 665 670 Gln Asn Val Leu Ser Leu Leu Arg         675 680 <210> 188 <211> 791 <212> PRT <213> Artificial Sequence <220> <223> HL982 STF2.D3Ins.HA1-L AH1 D3I-o1 <400> 188 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Ala Gln Asp Ile Leu Glu Lys Thr His Asn Gly         275 280 285 Lys Leu Cys Asp Leu Asp Gly Val Lys Pro Leu Ile Leu Arg Asp Cys     290 295 300 Ser Val Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile 305 310 315 320 Asn Val Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn                 325 330 335 Asp Leu Cys Tyr Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His             340 345 350 Leu Leu Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys         355 360 365 Ser Ser Trp Ser Asp His Glu Ala Ser Ser Gly Val Ser Ser Ala Cys     370 375 380 Pro Tyr Gln Gly Thr Pro Ser Phe Phe Arg Asn Val Val Trp Leu Ile 385 390 395 400 Lys Lys Asn Asn Thr Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr                 405 410 415 Asn Gln Glu Asp Leu Leu Ile Leu Trp Gly Ile His His Ser Asn Asp             420 425 430 Ala Ala Glu Gln Thr Lys Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser         435 440 445 Val Gly Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr     450 455 460 Arg Ser Lys Val Asn Gly Gln Ser Gly Arg Met Asp Phe Phe Trp Thr 465 470 475 480 Ile Leu Lys Pro Asn Asp Ile Asn Phe Glu Ser Asn Gly Asn Phe                 485 490 495 Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala             500 505 510 Ile Val Lys Ser Glu Val Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln         515 520 525 Thr Pro Ile Gly Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His     530 535 540 Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Lys Leu 545 550 555 560 Val Leu Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro                 565 570 575 Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val             580 585 590 Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr         595 600 605 Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly     610 615 620 Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys 625 630 635 640 Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala                 645 650 655 Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile             660 665 670 Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys         675 680 685 Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro     690 695 700 Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser 705 710 715 720 Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu                 725 730 735 Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp             740 745 750 Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu         755 760 765 Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln     770 775 780 Asn Val Leu Ser Leu Leu Arg 785 790 <210> 189 <211> 791 <212> PRT <213> Artificial Sequence <220> <223> HL960 STF2.D3Ins.HA1-L IND5 D3I-o1 <400> 189 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Ala Gln Asp Ile Leu Glu Lys Thr His Asn Gly         275 280 285 Lys Leu Cys Asp Leu Asp Gly Val Lys Pro Leu Ile Leu Arg Asp Cys     290 295 300 Ser Val Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile 305 310 315 320 Asn Val Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Thr Asn                 325 330 335 Asp Leu Cys Tyr Pro Gly Ser Phe Asn Asp Tyr Glu Glu Leu Lys His             340 345 350 Leu Leu Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys         355 360 365 Ser Ser Trp Ser Asp His Glu Ala Ser Ser Gly Val Ser Ser Ala Cys     370 375 380 Pro Tyr Leu Gly Ser Pro Ser Phe Phe Arg Asn Val Val Trp Leu Ile 385 390 395 400 Lys Lys Asn Ser Thr Tyr Pro Thr Ile Lys Lys Ser Tyr Asn Asn Thr                 405 410 415 Asn Gln Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp             420 425 430 Ala Ala Glu Gln Thr Arg Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser         435 440 445 Ile Gly Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr     450 455 460 Arg Ser Lys Val Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr 465 470 475 480 Ile Leu Lys Pro Asn Asp Ile Asn Phe Glu Ser Asn Gly Asn Phe                 485 490 495 Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala             500 505 510 Ile Met Lys Ser Glu Leu Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln         515 520 525 Thr Pro Met Gly Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His     530 535 540 Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Arg Leu 545 550 555 560 Val Leu Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro                 565 570 575 Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val             580 585 590 Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr         595 600 605 Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly     610 615 620 Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys 625 630 635 640 Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala                 645 650 655 Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile             660 665 670 Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys         675 680 685 Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro     690 695 700 Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser 705 710 715 720 Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu                 725 730 735 Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp             740 745 750 Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu         755 760 765 Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln     770 775 780 Asn Val Leu Ser Leu Leu Arg 785 790 <210> 190 <211> 777 <212> PRT <213> Artificial Sequence <220> <223> HL876 STF2.D3Ins.HA1-1L NY107 D31-o1 <400> 190 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Asn Ala Thr Glu Thr Val Glu Thr Thr Asn Ile Lys         275 280 285 Lys Ile Cys Thr Gln Gly Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly     290 295 300 Leu Leu Gly Thr Leu Ile Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu 305 310 315 320 Phe Ser Ser Asp Leu Ile Ile Glu Arg Arg Glu Gly Thr Asp Ile Cys                 325 330 335 Tyr Pro Gly Arg Phe Thr Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg             340 345 350 Arg Ser Gly Gly Ile Gly Lys Glu Ser Met Gly Phe Thr Tyr Ser Gly         355 360 365 Ile Arg Thr Asn Gly Ala Thr Ser Ala Cys Thr Arg Ser Ser Ser Ser Ser     370 375 380 Phe Tyr Ala Glu Met Lys Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala 385 390 395 400 Phe Pro Gln Met Thr Lys Ala Tyr Arg Asn Pro Arg Asn Lys Pro Ala                 405 410 415 Leu Ile Ile Trp Gly Val His His Ser Glu Ser Val Ser Glu Gln Thr             420 425 430 Lys Leu Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Arg Ser Ser Lys         435 440 445 Tyr Gln Gln Ser Phe Thr Pro Asn Pro Gly Ala Arg Arg Ile Asp Phe     450 455 460 His Trp Leu Leu Leu Asp Pro Asn Asp Thr Val Thr Phe Thr Phe Asn 465 470 475 480 Gly Ala Phe Ile Ala Pro Asp Arg Thr Ser Phe Phe Arg Gly Glu Ser                 485 490 495 Leu Gly Val Gln Ser Asp Ala Pro Leu Asp Ser Ser Cys Arg Gly Asp             500 505 510 Cys Phe His Ser Gly Gly Thr Ile Val Ser Ser Leu Pro Phe Gln Asn         515 520 525 Ile Asn Ser Arg Thr Val Gly Lys Cys Pro Arg Tyr Val Lys Gln Lys     530 535 540 Ser Leu Leu Leu Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp 545 550 555 560 Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly                 565 570 575 Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser             580 585 590 Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys         595 600 605 Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala     610 615 620 Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys 625 630 635 640 Thr Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val                 645 650 655 Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp             660 665 670 Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu         675 680 685 Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu     690 695 700 Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr 705 710 715 720 Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile                 725 730 735 Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln             740 745 750 Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val         755 760 765 Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 191 <211> 785 <212> PRT <213> Artificial Sequence <220> <223> HL926 STF2.D3Ins.HA1-1L CA504 D3I-o1 <400> 191 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Asn Ala Thr Glu Thr Val Glu Thr Val Asn Ile Lys         275 280 285 Lys Ile Cys Thr Gln Gly Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly     290 295 300 Leu Leu Gly Thr Leu Ile Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu 305 310 315 320 Phe Asp Ala Asn Leu Ile Ile Glu Arg Arg Glu Gly Thr Asp Val Cys                 325 330 335 Tyr Pro Gly Lys Phe Thr Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg             340 345 350 Gly Ser Gly Gly Ile Asp Lys Glu Ser Met Gly Phe Thr Tyr Ser Gly         355 360 365 Ile Arg Thr Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Gly Ser Ser     370 375 380 Phe Tyr Ala Glu Met Lys Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala 385 390 395 400 Phe Pro Gln Met Thr Lys Ser Tyr Arg Asn Pro Arg Asn Lys Pro Ala                 405 410 415 Leu Ile Ile Trp Gly Val His His Ser Gly Ser Ala Thr Glu Gln Thr             420 425 430 Lys Leu Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Lys         435 440 445 Tyr Gln Gln Ser Phe Thr Pro Ser Pro Gly Ala Arg Pro Gln Val Asn     450 455 460 Gly Gln Ser Gly Arg Ile Asp Phe His Trp Leu Leu Leu Asp Pro Asn 465 470 475 480 Asp Thr Thr Phe Thr Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg                 485 490 495 Ala Ser Phe Phe Arg Gly Glu Ser Leu Gly Val Gln Ser Asp Val Pro             500 505 510 Leu Asp Ser Gly Cys Glu Gly Asp Cys Phe His Ser Gly Gly Thr Ile         515 520 525 Val Ser Ser Leu Pro Phe Gln Asn Ile Asn Pro Arg Thr Val Gly Lys     530 535 540 Cys Pro Arg Tyr Val Lys Gln Thr Ser Leu Leu Leu Ala Thr Thr Lys 545 550 555 560 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp                 565 570 575 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn             580 585 590 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr         595 600 605 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala     610 615 620 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr 625 630 635 640 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly                 645 650 655 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn             660 665 670 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala         675 680 685 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala     690 695 700 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln 705 710 715 720 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn                 725 730 735 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu             740 745 750 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser         755 760 765 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu     770 775 780 Arg 785 <210> 192 <211> 785 <212> PRT <213> Artificial Sequence <220> <223> HL880 STF2.D3Ins.HA1-1L NL219 D3I-o1 <400> 192 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Asn Ala Thr Glu Thr Val Glu Arg Thr Asn Val Pro         275 280 285 Arg Ile Cys Ser Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly     290 295 300 Leu Leu Gly Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu 305 310 315 320 Phe Ser Ala Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys                 325 330 335 Tyr Pro Gly Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg             340 345 350 Glu Ser Gly Gly Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly         355 360 365 Ile Arg Thr Asn Gly Thr Thr Ser Ala Cys Arg Arg Ser Gly Ser Ser     370 375 380 Phe Tyr Ala Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala 385 390 395 400 Phe Pro Gln Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala                 405 410 415 Leu Ile Ile Trp Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr             420 425 430 Lys Leu Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn         435 440 445 Tyr Gln Gln Ser Phe Val Ser Ser Pro Gly Ala Arg Pro Gln Val Asn     450 455 460 Gly Gln Ser Gly Arg Ile Asp Phe His Trp Leu Ile Leu Asn Pro Asn 465 470 475 480 Asp Thr Val Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg                 485 490 495 Ala Ser Phe Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Glu Val Gln             500 505 510 Val Asp Ala Asn Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile         515 520 525 Ile Ser Asn Leu Pro Phe Gln Asn Ile Asn Ser Arg Ala Val Gly Lys     530 535 540 Cys Pro Arg Tyr Val Lys Gln Glu Ser Leu Leu Leu Ala Thr Thr Lys 545 550 555 560 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp                 565 570 575 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn             580 585 590 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr         595 600 605 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala     610 615 620 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr 625 630 635 640 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly                 645 650 655 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn             660 665 670 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala         675 680 685 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala     690 695 700 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln 705 710 715 720 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn                 725 730 735 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu             740 745 750 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser         755 760 765 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu     770 775 780 Arg 785 <210> 193 <211> 753 <212> PRT <213> Artificial Sequence <220> <223> HL958 STF2.D3Ins.HA1-2 B / HK / 259 extension <400> 193 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys         275 280 285 Cys Pro Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys     290 295 300 Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser             340 345 350 Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys         355 360 365 Ile Gly Thr Ser Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn Lys Thr 385 390 395 400 Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly                 405 410 415 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Thr Gln             420 425 430 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser         435 440 445 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro     450 455 460 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val 465 470 475 480 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln                 485 490 495 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser             500 505 510 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys         515 520 525 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp     530 535 540 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn 545 550 555 560 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr                 565 570 575 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala             580 585 590 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr         595 600 605 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly     610 615 620 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn 625 630 635 640 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala                 645 650 655 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala             660 665 670 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln         675 680 685 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn     690 695 700 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu 705 710 715 720 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser                 725 730 735 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu             740 745 750 Arg      <210> 194 <211> 721 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 PE16 D3I-o1 <400> 194 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ser Pro His Gln Ile Leu Asp Gly Lys Asn Cys Thr         275 280 285 Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn     290 295 300 Lys Lys Trp Asp Leu Phe Val Glu Arg Ser Lys Ala Tyr Ser Asn Cys 305 310 315 320 Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala                 325 330 335 Ser Ser Gly Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly             340 345 350 Val Thr Gln Asn Gly Thr Ser Ser Ala Cys Ile Arg Arg Ser Seryl Asn         355 360 365 Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr His Leu Asn Phe Lys Tyr     370 375 380 Pro Ala Leu Asn Val Thr Met Pro Asn Asn Glu Gln Phe Asp Lys Leu 385 390 395 400 Tyr Ile Trp Gly Val His His Pro Gly Thr Asp Lys Asp Gln Ile Phe                 405 410 415 Leu Tyr Ala Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser             420 425 430 Gln Gln Thr Val Ser Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asn         435 440 445 Ile Pro Ser Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp     450 455 460 Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr 465 470 475 480 Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Thr Lys                 485 490 495 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp             500 505 510 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn         515 520 525 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr     530 535 540 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala 545 550 555 560 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr                 565 570 575 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly             580 585 590 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn         595 600 605 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala     610 615 620 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala 625 630 635 640 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln                 645 650 655 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn             660 665 670 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu         675 680 685 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser     690 695 700 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu 705 710 715 720 Arg      <210> 195 <211> 770 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 PE16 D3I-o1 <400> 195 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gln Ser Ser Ser Thr Gly Glu Ile Cys Asp Ser Pro         275 280 285 His Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp Ala Leu Leu     290 295 300 Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe 305 310 315 320 Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro                 325 330 335 Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu             340 345 350 Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr         355 360 365 Ser Ser Ala Cys Ile Arg Ser Ser Lys Asn Ser Phe Ser Ser Le Le     370 375 380 Asn Trp Leu Thr His Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr 385 390 395 400 Met Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Ile Trp Gly Val His                 405 410 415 His Pro Gly Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ala Ser             420 425 430 Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ser Pro         435 440 445 Asn Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser Arg Ile Ser     450 455 460 Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser 465 470 475 480 Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly                 485 490 495 Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser             500 505 510 Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln         515 520 525 Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Thr     530 535 540 Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala 545 550 555 560 Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala                 565 570 575 Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys             580 585 590 Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala         595 600 605 Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser     610 615 620 Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Aspen Gln Aspen Gly 625 630 635 640 Gly Val Asp Gly Lys Thr Gly Val Val Thr Ile Asp Gly Lys Thr Tyr                 645 650 655 Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu             660 665 670 Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp         675 680 685 Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val     690 695 700 Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn 705 710 715 720 Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr                 725 730 735 Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr             740 745 750 Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu         755 760 765 Leu Arg     770 <210> 196 <211> 721 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 WY03 D3I-o1 <400> 196 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr         275 280 285 Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn     290 295 300 Lys Lys Trp Asp Leu Phe Val Glu Arg Ser Lys Ala Tyr Ser Asn Cys 305 310 315 320 Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala                 325 330 335 Ser Ser Gly Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Ala Gly             340 345 350 Val Thr Gln Asn Gly Thr Ser Ser Ala Cys Lys Arg Arg Ser Asn Lys         355 360 365 Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr His Leu Lys Tyr Lys Tyr     370 375 380 Pro Ala Leu Asn Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu 385 390 395 400 Tyr Ile Trp Gly Val His His Pro Val Thr Asp Ser Asp Gln Ile Ser                 405 410 415 Leu Tyr Ala Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser             420 425 430 Gln Gln Thr Val Ile Pro Asn Ile Gly Tyr Arg Pro Arg Val Arg Asp         435 440 445 Ile Ser Ser Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp     450 455 460 Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr 465 470 475 480 Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Thr Lys                 485 490 495 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp             500 505 510 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn         515 520 525 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr     530 535 540 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala 545 550 555 560 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr                 565 570 575 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly             580 585 590 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn         595 600 605 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala     610 615 620 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala 625 630 635 640 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln                 645 650 655 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn             660 665 670 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu         675 680 685 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser     690 695 700 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu 705 710 715 720 Arg      <210> 197 <211> 770 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 WY03 D3I-o1 <400> 197 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro         275 280 285 His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu     290 295 300 Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe 305 310 315 320 Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro                 325 330 335 Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu             340 345 350 Phe Asn Asn Glu Ser Phe Asn Trp Ala Gly Val Thr Gln Asn Gly Thr         355 360 365 Ser Ser Ala Cys Lys Arg Arg Ser Asn Lys Ser Phe Phe Ser Arg Leu     370 375 380 Asn Trp Leu Thr His Leu Lys Tyr Lys Tyr Pro Ala Leu Asn Val Thr 385 390 395 400 Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly Val His                 405 410 415 His Pro Val Thr Asp Ser Asp Gln Ile Ser Leu Tyr Ala Gln Ala Ser             420 425 430 Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro         435 440 445 Asn Ile Gly Tyr Arg Pro Arg Val Arg Asp Ile Ser Ser Arg Ile Ser     450 455 460 Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser 465 470 475 480 Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly                 485 490 495 Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser             500 505 510 Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln         515 520 525 Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Thr     530 535 540 Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala 545 550 555 560 Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala                 565 570 575 Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys             580 585 590 Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala         595 600 605 Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser     610 615 620 Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Aspen Gln Aspen Gly 625 630 635 640 Gly Val Asp Gly Lys Thr Gly Val Val Thr Ile Asp Gly Lys Thr Tyr                 645 650 655 Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu             660 665 670 Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp         675 680 685 Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val     690 695 700 Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn 705 710 715 720 Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr                 725 730 735 Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr             740 745 750 Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu         755 760 765 Leu Arg     770 <210> 198 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L WY03 D3I-o1 <400> 198 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys         275 280 285 Asp Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp 305 310 315 320 Asp Leu Phe Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Ala Gly Val Thr Gln         355 360 365 Asn Gly Thr Ser Ser Ala Cys Lys Arg Arg Ser Asn Lys Ser Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr His Leu Lys Tyr Lys Tyr Pro Ala Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp                 405 410 415 Gly Val His His Pro Val Thr Asp Ser Asp Gln Ile Ser Leu Tyr Ala             420 425 430 Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr         435 440 445 Val Ile Pro Asn Ile Gly Tyr Arg Pro Arg Val Arg Asp Ile Ser Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu 465 470 475 480 Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile                 485 490 495 Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys             500 505 510 Cys Asn Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr     530 535 540 Val Lys Gln Asn Thr Leu Lys Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 199 <211> 721 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 NY2782 D3I-o1 <400> 199 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr         275 280 285 Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn     290 295 300 Lys Lys Trp Asp Leu Phe Val Glu Arg Ser Lys Ala Tyr Ser Asn Cys 305 310 315 320 Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala                 325 330 335 Ser Ser Gly Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly             340 345 350 Val Thr Gln Asn Gly Thr Ser Ser Ala Cys Lys Arg Arg Ser Ser Ser         355 360 365 Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr His Leu Lys Phe Lys Tyr     370 375 380 Pro Ala Leu Asn Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu 385 390 395 400 Tyr Ile Trp Gly Val His His Pro Ser Thr Asp Asn Asp Gln Ile Ser                 405 410 415 Leu Tyr Ala Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser             420 425 430 Gln Gln Thr Val Ile Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asp         435 440 445 Ile Pro Ser Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp     450 455 460 Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr 465 470 475 480 Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Thr Lys                 485 490 495 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp             500 505 510 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn         515 520 525 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr     530 535 540 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala 545 550 555 560 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr                 565 570 575 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly             580 585 590 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn         595 600 605 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala     610 615 620 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala 625 630 635 640 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln                 645 650 655 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn             660 665 670 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu         675 680 685 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser     690 695 700 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu 705 710 715 720 Arg      <210> 200 <211> 770 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 NY2782 D3I-o1 <400> 200 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro         275 280 285 His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu     290 295 300 Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe 305 310 315 320 Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro                 325 330 335 Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu             340 345 350 Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr         355 360 365 Ser Ser Ala Cys Lys Arg Ser Ser Asn Ser Ser Phe Ser Ser Le Le     370 375 380 Asn Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu Asn Val Thr 385 390 395 400 Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly Val His                 405 410 415 His Pro Ser Thr Asp Asn Asp Gln Ile Ser Leu Tyr Ala Gln Ala Ser             420 425 430 Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro         435 440 445 Asn Ile Gly Ser Arg Pro Arg Val Arg Asp Ile Pro Ser Arg Ile Ser     450 455 460 Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser 465 470 475 480 Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly                 485 490 495 Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser             500 505 510 Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln         515 520 525 Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Thr     530 535 540 Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala 545 550 555 560 Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala                 565 570 575 Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys             580 585 590 Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala         595 600 605 Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser     610 615 620 Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Aspen Gln Aspen Gly 625 630 635 640 Gly Val Asp Gly Lys Thr Gly Val Val Thr Ile Asp Gly Lys Thr Tyr                 645 650 655 Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu             660 665 670 Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp         675 680 685 Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val     690 695 700 Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn 705 710 715 720 Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr                 725 730 735 Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr             740 745 750 Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu         755 760 765 Leu Arg     770 <210> 201 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L NY2782 D3I-o1 <400> 201 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys         275 280 285 Asp Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp 305 310 315 320 Asp Leu Phe Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln         355 360 365 Asn Gly Thr Ser Ser Ala Cys Lys Arg Ser Ser Asn Ser Ser Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp                 405 410 415 Gly Val His His Pro Ser Thr Asp Asn Asp Gln Ile Ser Leu Tyr Ala             420 425 430 Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr         435 440 445 Val Ile Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asp Ile Pro Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu 465 470 475 480 Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile                 485 490 495 Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys             500 505 510 Cys Asn Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr     530 535 540 Val Lys Gln Asn Thr Leu Lys Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 202 <211> 721 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 VT361 D3I-o1 <400> 202 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr         275 280 285 Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn     290 295 300 Lys Lys Trp Asp Leu Phe Val Glu Arg Ser Lys Ala Tyr Ser Asn Cys 305 310 315 320 Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala                 325 330 335 Ser Ser Gly Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly             340 345 350 Val Thr Gln Asn Gly Thr Ser Ser Ala Cys Ile Arg Arg Ser Asn Asn         355 360 365 Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr Gln Leu Asn Phe Lys Tyr     370 375 380 Pro Ala Leu Asn Val Thr Met Pro Asn Asn Glu Gln Phe Asp Lys Leu 385 390 395 400 Tyr Ile Trp Gly Val His His Pro Val Thr Asp Lys Asp Gln Ile Phe                 405 410 415 Leu Tyr Ala Gln Ser Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser             420 425 430 Gln Gln Ala Val Ile Pro Asn Ile Gly Tyr Arg Pro Arg Ile Arg Asn         435 440 445 Ile Pro Ser Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp     450 455 460 Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr 465 470 475 480 Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Thr Lys                 485 490 495 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp             500 505 510 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn         515 520 525 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr     530 535 540 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala 545 550 555 560 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr                 565 570 575 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly             580 585 590 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn         595 600 605 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala     610 615 620 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala 625 630 635 640 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln                 645 650 655 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn             660 665 670 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu         675 680 685 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser     690 695 700 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu 705 710 715 720 Arg      <210> 203 <211> 770 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 VT361 D3I-o1 <400> 203 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gln Asn Ser Ser Ile Gly Glu Ile Cys Asp Ser Pro         275 280 285 His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu     290 295 300 Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe 305 310 315 320 Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro                 325 330 335 Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu             340 345 350 Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr         355 360 365 Ser Ser Ala Cys Ile Arg Ser Ser Asn Ser Ser Phe Ser Arg Leu     370 375 380 Asn Trp Leu Thr Gln Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr 385 390 395 400 Met Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Ile Trp Gly Val His                 405 410 415 His Pro Val Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ser Ser             420 425 430 Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Ala Val Ile Pro         435 440 445 Asn Ile Gly Tyr Arg Pro Arg Ile Arg Asn Ile Pro Ser Arg Ile Ser     450 455 460 Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser 465 470 475 480 Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly                 485 490 495 Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser             500 505 510 Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln         515 520 525 Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Thr     530 535 540 Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala 545 550 555 560 Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala                 565 570 575 Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys             580 585 590 Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala         595 600 605 Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser     610 615 620 Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Aspen Gln Aspen Gly 625 630 635 640 Gly Val Asp Gly Lys Thr Gly Val Val Thr Ile Asp Gly Lys Thr Tyr                 645 650 655 Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu             660 665 670 Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp         675 680 685 Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val     690 695 700 Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn 705 710 715 720 Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr                 725 730 735 Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr             740 745 750 Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu         755 760 765 Leu Arg     770 <210> 204 <211> 721 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 Aichi2 D3I-o1 <400> 204 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Asn Pro His Arg Ile Leu Asp Gly Ile Asp Cys Thr         275 280 285 Leu Ile Asp Ala Leu Leu Gly Asp Pro His Cys Asp Val Phe Gln Asn     290 295 300 Glu Thr Trp Asp Leu Phe Val Glu Arg Ser Lys Ala Phe Ser Asn Cys 305 310 315 320 Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala                 325 330 335 Ser Ser Gly Thr Leu Glu Phe Ile Thr Glu Gly Phe Thr Trp Thr Gly             340 345 350 Val Thr Gln Asn Gly Gly Ser Asn Ala Cys Lys Arg Gly Pro Gly Ser         355 360 365 Gly Phe Phe Ser Arg Leu Asn Trp Leu Thr Lys Ser Gly Ser Thr Tyr     370 375 380 Pro Val Leu Asn Val Thr Met Pro Asn Asn Asp Asn Phe Asp Lys Leu 385 390 395 400 Tyr Ile Trp Gly Ile His His Pro Ser Thr Asn Gln Glu Gln Thr Ser                 405 410 415 Leu Tyr Val Gln Ala Ser Gly Arg Val Thr Val Ser Thr Arg Arg Ser             420 425 430 Gln Gln Thr Ile Ile Pro Asn Ile Gly Ser Arg Pro Trp Val Arg Gly         435 440 445 Leu Ser Ser Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp     450 455 460 Val Leu Val Ile Asn Ser Asn Gly Asn Leu Ile Ala Pro Arg Gly Tyr 465 470 475 480 Phe Lys Met Arg Thr Gly Lys Ser Ser Ile Met Arg Ser Asp Thr Lys                 485 490 495 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp             500 505 510 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn         515 520 525 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr     530 535 540 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala 545 550 555 560 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr                 565 570 575 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly             580 585 590 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn         595 600 605 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala     610 615 620 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala 625 630 635 640 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln                 645 650 655 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn             660 665 670 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu         675 680 685 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser     690 695 700 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu 705 710 715 720 Arg      <210> 205 <211> 770 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 Aichi2 D3I-o1 <400> 205 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gln Ser Ser Ser Thr Gly Lys Ile Cys Asn As Pro         275 280 285 His Arg Ile Leu Asp Gly Ile Asp Cys Thr Leu Ile Asp Ala Leu Leu     290 295 300 Gly Asp Pro His Cys Asp Val Phe Gln Asn Glu Thr Trp Asp Leu Phe 305 310 315 320 Val Glu Arg Ser Lys Ala Phe Ser Asn Cys Tyr Pro Tyr Asp Val Pro                 325 330 335 Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu             340 345 350 Phe Ile Thr Glu Gly Phe Thr Trp Thr Gly Val Thr Gln Asn Gly Gly         355 360 365 Ser Asn Ala Cys Lys Arg Gly Pro Gly Ser Gly Phe Ser Ser Leu     370 375 380 Asn Trp Leu Thr Lys Ser Gly Ser Thr Tyr Pro Val Leu Asn Val Thr 385 390 395 400 Met Pro Asn Asn Asp Asn Phe Asp Lys Leu Tyr Ile Trp Gly Ile His                 405 410 415 His Pro Ser Thr Asn Gln Glu Gln Thr Ser Leu Tyr Val Gln Ala Ser             420 425 430 Gly Arg Val Thr Val Ser Thr Arg Arg Ser Gln Gln Thr Ile Ile Pro         435 440 445 Asn Ile Gly Ser Arg Pro Trp Val Arg Gly Leu Ser Ser Arg Ile Ser     450 455 460 Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Val Leu Val Ile Asn Ser 465 470 475 480 Asn Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Met Arg Thr Gly                 485 490 495 Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Asp Thr Cys Ile Ser             500 505 510 Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln         515 520 525 Asn Val Asn Lys Ile Thr Tyr Gly Ala Cys Pro Lys Tyr Val Lys Thr     530 535 540 Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala 545 550 555 560 Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala                 565 570 575 Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys             580 585 590 Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala         595 600 605 Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser     610 615 620 Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Aspen Gln Aspen Gly 625 630 635 640 Gly Val Asp Gly Lys Thr Gly Val Val Thr Ile Asp Gly Lys Thr Tyr                 645 650 655 Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu             660 665 670 Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp         675 680 685 Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val     690 695 700 Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn 705 710 715 720 Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr                 725 730 735 Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr             740 745 750 Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu         755 760 765 Leu Arg     770 <210> 206 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L Aichi2 D3I-o1 <400> 206 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Lys Ile Cys         275 280 285 Asn Asn Pro His Arg Ile Leu Asp Gly Ile Asp Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro His Cys Asp Val Phe Gln Asn Glu Thr Trp 305 310 315 320 Asp Leu Phe Val Glu Arg Ser Lys Ala Phe Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Ile Thr Glu Gly Phe Thr Trp Thr Gly Val Thr Gln         355 360 365 Asn Gly Gly Ser Asn Ala Cys Lys Arg Gly Pro Gly Ser Gly Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr Lys Ser Gly Ser Thr Tyr Pro Val Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Asp Asn Phe Asp Lys Leu Tyr Ile Trp                 405 410 415 Gly Ile His His Pro Ser Thr Asn Gln Glu Gln Thr Ser Leu Tyr Val             420 425 430 Gln Ala Ser Gly Arg Val Thr Val Ser Thr Arg Arg Ser Gln Gln Thr         435 440 445 Ile Ile Pro Asn Ile Gly Ser Arg Pro Trp Val Arg Gly Leu Ser Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Val Leu Val 465 470 475 480 Ile Asn Ser Asn Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Met                 485 490 495 Arg Thr Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Asp Thr             500 505 510 Cys Ile Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Lys Ile Thr Tyr Gly Ala Cys Pro Lys Tyr     530 535 540 Val Lys Gln Asn Thr Leu Lys Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 207 <211> 721 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 WI67 D3I-o1 <400> 207 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr         275 280 285 Leu Ile Asp Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn     290 295 300 Lys Lys Trp Asp Leu Phe Val Glu Arg Ser Lys Ala Tyr Ser Asn Cys 305 310 315 320 Tyr Pro Tyr Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala                 325 330 335 Ser Ser Gly Thr Leu Glu Phe Asn Asp Glu Ser Phe Asn Trp Thr Gly             340 345 350 Val Thr Gln Asn Gly Thr Ser Ser Ala Cys Lys Arg Arg Ser Asn Asn         355 360 365 Ser Phe Phe Ser Arg Leu Asn Trp Leu Thr His Leu Lys Phe Lys Tyr     370 375 380 Pro Ala Leu Asn Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu 385 390 395 400 Tyr Ile Trp Gly Val His His Pro Gly Thr Asp Asn Asp Gln Ile Phe                 405 410 415 Leu His Ala Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser             420 425 430 Gln Gln Thr Val Ile Pro Asn Ile Gly Ser Arg Pro Arg Ile Arg Asn         435 440 445 Ile Pro Ser Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp     450 455 460 Ile Leu Leu Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr 465 470 475 480 Phe Lys Ile Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Thr Lys                 485 490 495 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp             500 505 510 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn         515 520 525 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr     530 535 540 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala 545 550 555 560 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr                 565 570 575 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly             580 585 590 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn         595 600 605 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala     610 615 620 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala 625 630 635 640 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln                 645 650 655 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn             660 665 670 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu         675 680 685 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser     690 695 700 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu 705 710 715 720 Arg      <210> 208 <211> 770 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 WI67 D3I-o1 <400> 208 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro         275 280 285 His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu     290 295 300 Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Phe 305 310 315 320 Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro                 325 330 335 Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu             340 345 350 Phe Asn Asp Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr         355 360 365 Ser Ser Ala Cys Lys Arg Arg Ser Asn Asn Ser Phe Ser Ser Leu     370 375 380 Asn Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu Asn Val Thr 385 390 395 400 Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp Gly Val His                 405 410 415 His Pro Gly Thr Asp Asn Asp Gln Ile Phe Leu His Ala Gln Ala Ser             420 425 430 Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro         435 440 445 Asn Ile Gly Ser Arg Pro Arg Ile Arg Asn Ile Pro Ser Arg Ile Ser     450 455 460 Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser 465 470 475 480 Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly                 485 490 495 Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser             500 505 510 Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln         515 520 525 Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Thr     530 535 540 Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala 545 550 555 560 Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala                 565 570 575 Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys             580 585 590 Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala         595 600 605 Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser     610 615 620 Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Aspen Gln Aspen Gly 625 630 635 640 Gly Val Asp Gly Lys Thr Gly Val Val Thr Ile Asp Gly Lys Thr Tyr                 645 650 655 Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu             660 665 670 Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp         675 680 685 Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val     690 695 700 Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn 705 710 715 720 Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr                 725 730 735 Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr             740 745 750 Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu         755 760 765 Leu Arg     770 <210> 209 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L WI67 D3I-o1 <400> 209 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys         275 280 285 Asp Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp 305 310 315 320 Asp Leu Phe Val Glu Arg Ser Ser Ays Tyr Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Asn Asp Glu Ser Phe Asn Trp Thr Gly Val Thr Gln         355 360 365 Asn Gly Thr Ser Ser Ala Cys Lys Arg Arg Ser Asn Ser Ser Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Ile Trp                 405 410 415 Gly Val His His Pro Gly Thr Asp Asn Asp Gln Ile Phe Leu His Ala             420 425 430 Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr         435 440 445 Val Ile Pro Asn Ile Gly Ser Arg Pro Arg Ile Arg Asn Ile Pro Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu 465 470 475 480 Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile                 485 490 495 Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys             500 505 510 Cys Asn Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr     530 535 540 Val Lys Gln Asn Thr Leu Lys Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 210 <211> 726 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 AH1 D3I-o1 <400> 210 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val         275 280 285 Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val     290 295 300 Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn Asp Leu 305 310 315 320 Cys Tyr Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu                 325 330 335 Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser             340 345 350 Trp Ser Asp His Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr         355 360 365 Gln Gly Thr Pro Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys     370 375 380 Asn Asn Thr Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln 385 390 395 400 Glu Asp Leu Leu Ile Leu Trp Gly Ile His His Ser Asn Asp Ala Ala                 405 410 415 Glu Gln Thr Lys Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly             420 425 430 Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser         435 440 445 Lys Val Asn Gly Gln Ser Gly Arg Met Asp Phe Phe Trp Thr Ile Leu     450 455 460 Lys Pro Asn Asp Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala 465 470 475 480 Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala Ile Val                 485 490 495 Lys Ser Glu Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala             500 505 510 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp         515 520 525 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp     530 535 540 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp 545 550 555 560 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala                 565 570 575 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala             580 585 590 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp         595 600 605 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala     610 615 620 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu 625 630 635 640 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp                 645 650 655 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly             660 665 670 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser         675 680 685 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln     690 695 700 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn 705 710 715 720 Val Leu Ser Leu Leu Arg                 725 <210> 211 <211> 777 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 AH1 D3I-o1 <400> 211 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Lys Thr His Asn Gly Lys Leu Cys Asp Leu Asp         275 280 285 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu     290 295 300 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn Asp Leu Cys Tyr Pro Gly                 325 330 335 Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn             340 345 350 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His         355 360 365 Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly Thr Pro     370 375 380 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Asn Thr Tyr 385 390 395 400 Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu                 405 410 415 Ile Leu Trp Gly Ile His His Ser Asn Asp Ala Ala Glu Gln Thr Lys             420 425 430 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser Thr Leu         435 440 445 Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Val Asn Gly     450 455 460 Gln Ser Gly Arg Met Asp Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp 465 470 475 480 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala                 485 490 495 Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala Ile Val Lys Ser Glu Val             500 505 510 Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Ile Gly Ala Ile         515 520 525 Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu     530 535 540 Cys Pro Lys Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp 545 550 555 560 Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly                 565 570 575 Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser             580 585 590 Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys         595 600 605 Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala     610 615 620 Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys 625 630 635 640 Thr Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val                 645 650 655 Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp             660 665 670 Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu         675 680 685 Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu     690 695 700 Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr 705 710 715 720 Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile                 725 730 735 Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln             740 745 750 Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val         755 760 765 Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 212 <211> 726 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 QH1A D3I-o1 <400> 212 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val         275 280 285 Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Leu Asn Val     290 295 300 Pro Glu Trp Ser Tyr Ile Val Glu Lys Ile Asn Pro Ala Asn Asp Leu 305 310 315 320 Cys Tyr Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu                 325 330 335 Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser             340 345 350 Trp Ser Asp His Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr         355 360 365 Gln Gly Arg Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys     370 375 380 Asn Asn Ala Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln 385 390 395 400 Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala                 405 410 415 Glu Gln Thr Arg Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly             420 425 430 Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser         435 440 445 Lys Val Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu     450 455 460 Lys Pro Asn Asp Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala 465 470 475 480 Pro Glu Asn Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met                 485 490 495 Lys Ser Glu Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala             500 505 510 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp         515 520 525 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp     530 535 540 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp 545 550 555 560 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala                 565 570 575 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala             580 585 590 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp         595 600 605 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala     610 615 620 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu 625 630 635 640 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp                 645 650 655 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly             660 665 670 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser         675 680 685 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln     690 695 700 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn 705 710 715 720 Val Leu Ser Leu Leu Arg                 725 <210> 213 <211> 777 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 QH1A D3I-o1 <400> 213 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Lys Thr His Asn Gly Lys Leu Cys Asp Leu Asp         275 280 285 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu     290 295 300 Leu Gly Asn Pro Met Cys Asp Glu Phe Leu Asn Val Pro Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Lys Ile Asn Pro Ala Asn Asp Leu Cys Tyr Pro Gly                 325 330 335 Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn             340 345 350 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His         355 360 365 Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly Arg Ser     370 375 380 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Asn Ala Tyr 385 390 395 400 Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu                 405 410 415 Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Arg             420 425 430 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser Thr Leu         435 440 445 Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Val Asn Gly     450 455 460 Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp 465 470 475 480 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Asn Ala                 485 490 495 Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu Leu             500 505 510 Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Ile Gly Ala Ile         515 520 525 Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu     530 535 540 Cys Pro Lys Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp 545 550 555 560 Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly                 565 570 575 Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser             580 585 590 Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys         595 600 605 Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala     610 615 620 Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys 625 630 635 640 Thr Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val                 645 650 655 Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp             660 665 670 Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu         675 680 685 Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu     690 695 700 Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr 705 710 715 720 Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile                 725 730 735 Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln             740 745 750 Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val         755 760 765 Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 214 <211> 791 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L QH1A D3I-o1 <400> 214 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Ala Gln Asp Ile Leu Glu Lys Thr His Asn Gly         275 280 285 Lys Leu Cys Asp Leu Asp Gly Val Lys Pro Leu Ile Leu Arg Asp Cys     290 295 300 Ser Val Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Leu 305 310 315 320 Asn Val Pro Glu Trp Ser Tyr Ile Val Glu Lys Ile Asn Pro Ala Asn                 325 330 335 Asp Leu Cys Tyr Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His             340 345 350 Leu Leu Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys         355 360 365 Ser Ser Trp Ser Asp His Glu Ala Ser Ser Gly Val Ser Ser Ala Cys     370 375 380 Pro Tyr Gln Gly Arg Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile 385 390 395 400 Lys Lys Asn Asn Ala Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr                 405 410 415 Asn Gln Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp             420 425 430 Ala Ala Glu Gln Thr Arg Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser         435 440 445 Val Gly Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr     450 455 460 Arg Ser Lys Val Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr 465 470 475 480 Ile Leu Lys Pro Asn Asp Ile Asn Phe Glu Ser Asn Gly Asn Phe                 485 490 495 Ile Ala Pro Glu Asn Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr             500 505 510 Ile Met Lys Ser Glu Leu Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln         515 520 525 Thr Pro Ile Gly Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His     530 535 540 Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Arg Leu 545 550 555 560 Val Leu Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro                 565 570 575 Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val             580 585 590 Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr         595 600 605 Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly     610 615 620 Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys 625 630 635 640 Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala                 645 650 655 Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile             660 665 670 Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys         675 680 685 Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro     690 695 700 Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser 705 710 715 720 Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu                 725 730 735 Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp             740 745 750 Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu         755 760 765 Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln     770 775 780 Asn Val Leu Ser Leu Leu Arg 785 790 <210> 215 <211> 726 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 IND5 D3I-o1 <400> 215 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val         275 280 285 Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val     290 295 300 Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Thr Asn Asp Leu 305 310 315 320 Cys Tyr Pro Gly Ser Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu                 325 330 335 Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser             340 345 350 Trp Ser Asp His Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr         355 360 365 Leu Gly Ser Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys     370 375 380 Asn Ser Thr Tyr Pro Thr Ile Lys Lys Ser Tyr Asn Asn Thr Asn Gln 385 390 395 400 Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala                 405 410 415 Glu Gln Thr Arg Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Ile Gly             420 425 430 Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser         435 440 445 Lys Val Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu     450 455 460 Lys Pro Asn Asp Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala 465 470 475 480 Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala Ile Met                 485 490 495 Lys Ser Glu Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala             500 505 510 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp         515 520 525 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp     530 535 540 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp 545 550 555 560 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala                 565 570 575 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala             580 585 590 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp         595 600 605 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala     610 615 620 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu 625 630 635 640 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp                 645 650 655 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly             660 665 670 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser         675 680 685 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln     690 695 700 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn 705 710 715 720 Val Leu Ser Leu Leu Arg                 725 <210> 216 <211> 777 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 IND5 D3I-o1 <400> 216 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Lys Thr His Asn Gly Lys Leu Cys Asp Leu Asp         275 280 285 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu     290 295 300 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Lys Ala Asn Pro Thr Asn Leu Cys Tyr Pro Gly                 325 330 335 Ser Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn             340 345 350 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asp His         355 360 365 Glu Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Leu Gly Ser Pro     370 375 380 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser Thr Tyr 385 390 395 400 Pro Thr Ile Lys Lys Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu                 405 410 415 Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Arg             420 425 430 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Ile Gly Thr Ser Thr Leu         435 440 445 Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Val Asn Gly     450 455 460 Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp 465 470 475 480 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala                 485 490 495 Tyr Lys Ile Val Lys Lys Gly Asp Ser Ala Ile Met Lys Ser Glu Leu             500 505 510 Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Met Gly Ala Ile         515 520 525 Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu     530 535 540 Cys Pro Lys Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp 545 550 555 560 Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly                 565 570 575 Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser             580 585 590 Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys         595 600 605 Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala     610 615 620 Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys 625 630 635 640 Thr Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val                 645 650 655 Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp             660 665 670 Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu         675 680 685 Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu     690 695 700 Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr 705 710 715 720 Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile                 725 730 735 Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln             740 745 750 Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val         755 760 765 Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 217 <211> 726 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 VN1203 D3I-o1 <400> 217 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val         275 280 285 Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val     290 295 300 Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Val Asn Asp Leu 305 310 315 320 Cys Tyr Pro Gly Asp Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu                 325 330 335 Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser             340 345 350 Trp Ser Ser His Glu Ala Ser Leu Gly Val Ser Ser Ala Cys Pro Tyr         355 360 365 Gln Gly Lys Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys     370 375 380 Asn Ser Thr Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln 385 390 395 400 Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala                 405 410 415 Glu Gln Thr Lys Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly             420 425 430 Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Arg Ile Ala Thr Arg Ser         435 440 445 Lys Val Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu     450 455 460 Lys Pro Asn Asp Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala 465 470 475 480 Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met                 485 490 495 Lys Ser Glu Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala             500 505 510 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp         515 520 525 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp     530 535 540 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp 545 550 555 560 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala                 565 570 575 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala             580 585 590 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp         595 600 605 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala     610 615 620 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu 625 630 635 640 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp                 645 650 655 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly             660 665 670 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser         675 680 685 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln     690 695 700 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn 705 710 715 720 Val Leu Ser Leu Leu Arg                 725 <210> 218 <211> 777 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 VN1203 D3I-o1 <400> 218 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Lys Lys His Asn Gly Lys Leu Cys Asp Leu Asp         275 280 285 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu     290 295 300 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Lys Ala Asn Pro Val Asn Asp Leu Cys Tyr Pro Gly                 325 330 335 Asp Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn             340 345 350 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Ser His         355 360 365 Glu Ala Ser Leu Gly Val Ser Ser Ala Cys Pro Tyr Gln Gly Lys Ser     370 375 380 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser Thr Tyr 385 390 395 400 Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu                 405 410 415 Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Lys             420 425 430 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser Thr Leu         435 440 445 Asn Gln Arg Leu Val Pro Arg Ile Ala Thr Arg Ser Lys Val Asn Gly     450 455 460 Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp 465 470 475 480 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala                 485 490 495 Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu Leu             500 505 510 Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Met Gly Ala Ile         515 520 525 Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu     530 535 540 Cys Pro Lys Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp 545 550 555 560 Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly                 565 570 575 Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser             580 585 590 Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys         595 600 605 Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala     610 615 620 Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys 625 630 635 640 Thr Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val                 645 650 655 Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp             660 665 670 Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu         675 680 685 Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu     690 695 700 Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr 705 710 715 720 Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile                 725 730 735 Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln             740 745 750 Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val         755 760 765 Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 219 <211> 791 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L VN1203 D3I-o1 <400> 219 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Ala Gln Asp Ile Leu Glu Lys Lys His Asn Gly         275 280 285 Lys Leu Cys Asp Leu Asp Gly Val Lys Pro Leu Ile Leu Arg Asp Cys     290 295 300 Ser Val Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile 305 310 315 320 Asn Val Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Val Asn                 325 330 335 Asp Leu Cys Tyr Pro Gly Asp Phe Asn Asp Tyr Glu Glu Leu Lys His             340 345 350 Leu Leu Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys         355 360 365 Ser Ser Trp Ser Ser His Glu Ala Ser Leu Gly Val Ser Ser Ala Cys     370 375 380 Pro Tyr Gln Gly Lys Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile 385 390 395 400 Lys Lys Asn Ser Thr Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr                 405 410 415 Asn Gln Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp             420 425 430 Ala Ala Glu Gln Thr Lys Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser         435 440 445 Val Gly Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Arg Ile Ala Thr     450 455 460 Arg Ser Lys Val Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr 465 470 475 480 Ile Leu Lys Pro Asn Asp Ile Asn Phe Glu Ser Asn Gly Asn Phe                 485 490 495 Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr             500 505 510 Ile Met Lys Ser Glu Leu Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln         515 520 525 Thr Pro Met Gly Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His     530 535 540 Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Arg Leu 545 550 555 560 Val Leu Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro                 565 570 575 Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val             580 585 590 Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr         595 600 605 Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly     610 615 620 Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys 625 630 635 640 Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala                 645 650 655 Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile             660 665 670 Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys         675 680 685 Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro     690 695 700 Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser 705 710 715 720 Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu                 725 730 735 Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp             740 745 750 Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu         755 760 765 Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln     770 775 780 Asn Val Leu Ser Leu Leu Arg 785 790 <210> 220 <211> 726 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 HB1 D3I-o1 <400> 220 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Val Lys Pro Leu Ile Leu Lys Asp Cys Ser Val         275 280 285 Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val     290 295 300 Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn Asp Leu 305 310 315 320 Cys Tyr Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu                 325 330 335 Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Asn Ser             340 345 350 Trp Ser Asp His Glu Ala Ser Leu Gly Val Ser Ala Ala Cys Pro Tyr         355 360 365 Gln Gly Lys Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys     370 375 380 Asp Asn Ala Tyr Pro Thr Ile Lys Lys Gly Tyr Asn Asn Thr Asn Gln 385 390 395 400 Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Glu Ala                 405 410 415 Glu Gln Thr Arg Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Ile Gly             420 425 430 Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser         435 440 445 Lys Ile Asn Gly Gln Ser Gly Arg Ile Asp Phe Phe Trp Thr Ile Leu     450 455 460 Lys Pro Asn Asp Ala Ile His Phe Glu Ser Asn Gly Asn Phe Ile Ala 465 470 475 480 Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met                 485 490 495 Lys Ser Glu Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala             500 505 510 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp         515 520 525 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp     530 535 540 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp 545 550 555 560 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala                 565 570 575 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala             580 585 590 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp         595 600 605 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala     610 615 620 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu 625 630 635 640 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp                 645 650 655 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly             660 665 670 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser         675 680 685 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln     690 695 700 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn 705 710 715 720 Val Leu Ser Leu Leu Arg                 725 <210> 221 <211> 777 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 HB1 D3I-o1 <400> 221 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Lys Thr His Asn Gly Lys Leu Cys Asp Leu Asn         275 280 285 Gly Val Lys Pro Leu Ile Leu Lys Asp Cys Ser Val Ala Gly Trp Leu     290 295 300 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn Asp Leu Cys Tyr Pro Gly                 325 330 335 Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn             340 345 350 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Asn Ser Trp Ser Asp His         355 360 365 Glu Ala Ser Leu Gly Val Ser Ala Ala Cys Pro Tyr Gln Gly Lys Ser     370 375 380 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asp Asn Ala Tyr 385 390 395 400 Pro Thr Ile Lys Lys Gly Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu                 405 410 415 Val Leu Trp Gly Ile His His Pro Asn Asp Glu Ala Glu Gln Thr Arg             420 425 430 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Ile Gly Thr Ser Thr Leu         435 440 445 Asn Gln Arg Leu Val Pro Lys Ile Ala Thr Arg Ser Lys Ile Asn Gly     450 455 460 Gln Ser Gly Arg Ile Asp Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp 465 470 475 480 Ala Ile His Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala                 485 490 495 Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu Val             500 505 510 Glu Tyr Gly Asn Cys Asn Thr Arg Cys Gln Thr Pro Ile Gly Ala Ile         515 520 525 Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu     530 535 540 Cys Pro Lys Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp 545 550 555 560 Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly                 565 570 575 Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser             580 585 590 Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys         595 600 605 Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala     610 615 620 Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys 625 630 635 640 Thr Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val                 645 650 655 Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp             660 665 670 Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu         675 680 685 Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu     690 695 700 Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr 705 710 715 720 Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile                 725 730 735 Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln             740 745 750 Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val         755 760 765 Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 222 <211> 791 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L HB1 D3I-o1 <400> 222 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Ala Gln Asp Ile Leu Glu Lys Thr His Asn Gly         275 280 285 Lys Leu Cys Asp Leu Asn Gly Val Lys Pro Leu Ile Leu Lys Asp Cys     290 295 300 Ser Val Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile 305 310 315 320 Asn Val Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Asn Pro Ala Asn                 325 330 335 Asp Leu Cys Tyr Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His             340 345 350 Leu Leu Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys         355 360 365 Asn Ser Trp Ser Asp His Glu Ala Ser Leu Gly Val Ser Ala Ala Cys     370 375 380 Pro Tyr Gln Gly Lys Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile 385 390 395 400 Lys Lys Asp Asn Ala Tyr Pro Thr Ile Lys Lys Gly Tyr Asn Asn Thr                 405 410 415 Asn Gln Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp             420 425 430 Glu Ala Glu Gln Thr Arg Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser         435 440 445 Ile Gly Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Lys Ile Ala Thr     450 455 460 Arg Ser Lys Ile Asn Gly Gln Ser Gly Arg Ile Asp Phe Phe Trp Thr 465 470 475 480 Ile Leu Lys Pro Asn Asp Ala Ile His Phe Glu Ser Asn Gly Asn Phe                 485 490 495 Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr             500 505 510 Ile Met Lys Ser Glu Val Glu Tyr Gly Asn Cys Asn Thr Arg Cys Gln         515 520 525 Thr Pro Ile Gly Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His     530 535 540 Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Lys Leu 545 550 555 560 Val Leu Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro                 565 570 575 Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val             580 585 590 Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr         595 600 605 Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly     610 615 620 Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys 625 630 635 640 Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala                 645 650 655 Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile             660 665 670 Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys         675 680 685 Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro     690 695 700 Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser 705 710 715 720 Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu                 725 730 735 Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp             740 745 750 Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu         755 760 765 Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln     770 775 780 Asn Val Leu Ser Leu Leu Arg 785 790 <210> 223 <211> 726 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 HK156 D3I-o1 <400> 223 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val         275 280 285 Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val     290 295 300 Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Ser Pro Ala Asn Asp Leu 305 310 315 320 Cys Tyr Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu                 325 330 335 Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser             340 345 350 Trp Ser Asn His Asp Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr         355 360 365 Leu Gly Arg Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys     370 375 380 Asn Ser Ala Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln 385 390 395 400 Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala                 405 410 415 Glu Gln Thr Lys Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly             420 425 430 Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Glu Ile Ala Thr Arg Pro         435 440 445 Lys Val Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu     450 455 460 Lys Pro Asn Asp Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala 465 470 475 480 Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met                 485 490 495 Lys Ser Glu Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala             500 505 510 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp         515 520 525 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp     530 535 540 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp 545 550 555 560 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala                 565 570 575 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala             580 585 590 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp         595 600 605 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala     610 615 620 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu 625 630 635 640 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp                 645 650 655 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly             660 665 670 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser         675 680 685 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln     690 695 700 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn 705 710 715 720 Val Leu Ser Leu Leu Arg                 725 <210> 224 <211> 777 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 HK156 D3I-o1 <400> 224 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Arg Thr His Asn Gly Lys Leu Cys Asp Leu Asn         275 280 285 Gly Val Lys Pro Leu Ile Leu Arg Asp Cys Ser Val Ala Gly Trp Leu     290 295 300 Leu Gly Asn Pro Met Cys Asp Glu Phe Ile Asn Val Pro Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Lys Ala Ser Pro Ala Asn Asp Leu Cys Tyr Pro Gly                 325 330 335 Asn Phe Asn Asp Tyr Glu Glu Leu Lys His Leu Leu Ser Arg Ile Asn             340 345 350 His Phe Glu Lys Ile Gln Ile Ile Pro Lys Ser Ser Trp Ser Asn His         355 360 365 Asp Ala Ser Ser Gly Val Ser Ser Ala Cys Pro Tyr Leu Gly Arg Ser     370 375 380 Ser Phe Phe Arg Asn Val Val Trp Leu Ile Lys Lys Asn Ser Ala Tyr 385 390 395 400 Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu                 405 410 415 Val Leu Trp Gly Ile His His Pro Asn Asp Ala Ala Glu Gln Thr Lys             420 425 430 Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser Val Gly Thr Ser Thr Leu         435 440 445 Asn Gln Arg Leu Val Pro Glu Ile Ala Thr Arg Pro Lys Val Asn Gly     450 455 460 Gln Ser Gly Arg Met Glu Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp 465 470 475 480 Ala Ile Asn Phe Glu Ser Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala                 485 490 495 Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr Ile Met Lys Ser Glu Leu             500 505 510 Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln Thr Pro Met Gly Ala Ile         515 520 525 Asn Ser Ser Met Pro Phe His Asn Ile His Pro Leu Thr Ile Gly Glu     530 535 540 Cys Pro Lys Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp 545 550 555 560 Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly                 565 570 575 Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser             580 585 590 Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys         595 600 605 Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala     610 615 620 Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys 625 630 635 640 Thr Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val                 645 650 655 Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp             660 665 670 Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu         675 680 685 Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu     690 695 700 Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr 705 710 715 720 Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile                 725 730 735 Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln             740 745 750 Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val         755 760 765 Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 225 <211> 791 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L HK156 D3I-o1 <400> 225 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Ala Gln Asp Ile Leu Glu Arg Thr His Asn Gly         275 280 285 Lys Leu Cys Asp Leu Asn Gly Val Lys Pro Leu Ile Leu Arg Asp Cys     290 295 300 Ser Val Ala Gly Trp Leu Leu Gly Asn Pro Met Cys Asp Glu Phe Ile 305 310 315 320 Asn Val Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala Ser Pro Ala Asn                 325 330 335 Asp Leu Cys Tyr Pro Gly Asn Phe Asn Asp Tyr Glu Glu Leu Lys His             340 345 350 Leu Leu Ser Arg Ile Asn His Phe Glu Lys Ile Gln Ile Ile Pro Lys         355 360 365 Ser Ser Trp Ser Asn His Asp Ala Ser Ser Gly Val Ser Ser Ala Cys     370 375 380 Pro Tyr Leu Gly Arg Ser Ser Phe Phe Arg Asn Val Val Trp Leu Ile 385 390 395 400 Lys Lys Asn Ser Ala Tyr Pro Thr Ile Lys Arg Ser Tyr Asn Asn Thr                 405 410 415 Asn Gln Glu Asp Leu Leu Val Leu Trp Gly Ile His His Pro Asn Asp             420 425 430 Ala Ala Glu Gln Thr Lys Leu Tyr Gln Asn Pro Thr Thr Tyr Ile Ser         435 440 445 Val Gly Thr Ser Thr Leu Asn Gln Arg Leu Val Pro Glu Ile Ala Thr     450 455 460 Arg Pro Lys Val Asn Gly Gln Ser Gly Arg Met Glu Phe Phe Trp Thr 465 470 475 480 Ile Leu Lys Pro Asn Asp Ile Asn Phe Glu Ser Asn Gly Asn Phe                 485 490 495 Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys Gly Asp Ser Thr             500 505 510 Ile Met Lys Ser Glu Leu Glu Tyr Gly Asn Cys Asn Thr Lys Cys Gln         515 520 525 Thr Pro Met Gly Ala Ile Asn Ser Ser Met Pro Phe His Asn Ile His     530 535 540 Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr Val Lys Ser Asn Arg Leu 545 550 555 560 Val Leu Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro                 565 570 575 Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val             580 585 590 Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr         595 600 605 Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly     610 615 620 Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys 625 630 635 640 Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala                 645 650 655 Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile             660 665 670 Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys         675 680 685 Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro     690 695 700 Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser 705 710 715 720 Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu                 725 730 735 Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp             740 745 750 Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu         755 760 765 Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln     770 775 780 Asn Val Leu Ser Leu Leu Arg 785 790 <210> 226 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 AH1 D3I-o1 <400> 226 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu         275 280 285 Gly Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser     290 295 300 Ala Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro 305 310 315 320 Gly Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser                 325 330 335 Gly Gly Ile Asp Lys Glu Ala Met Gly Phe Thr Tyr Ser Gly Ile Arg             340 345 350 Thr Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr         355 360 365 Ala Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro     370 375 380 Gln Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Ser Pro Ala Leu Ile 385 390 395 400 Val Trp Gly Ile His His Ser Val Ser Thr Ala Glu Gln Thr Lys Leu                 405 410 415 Tyr Gly Ser Gly Asn Lys Leu Val Thr Val Gly Ser Ser Asn Tyr Gln             420 425 430 Gln Ser Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Leu         435 440 445 Ser Gly Arg Ile Asp Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr     450 455 460 Val Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser 465 470 475 480 Phe Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Gly Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 227 <211> 774 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 AH1 D3I-o1 <400> 227 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Thr Val Glu Arg Thr Asn Ile Pro Arg Ile Cys         275 280 285 Ser Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly     290 295 300 Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala 305 310 315 320 Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly                 325 330 335 Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly             340 345 350 Gly Ile Asp Lys Glu Ala Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr         355 360 365 Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr Ala     370 375 380 Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln 385 390 395 400 Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Ser Pro Ala Leu Ile Val                 405 410 415 Trp Gly Ile His His Ser Val Ser Thr Ala Glu Gln Thr Lys Leu Tyr             420 425 430 Gly Ser Gly Asn Lys Leu Val Thr Val Gly Ser Ser Asn Tyr Gln Gln         435 440 445 Ser Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Leu Ser     450 455 460 Gly Arg Ile Asp Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr Val 465 470 475 480 Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe                 485 490 495 Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Gly Val Gln Val Asp Ala             500 505 510 Asn Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn         515 520 525 Leu Pro Phe Gln Asn Ile Asp Ser Arg Ala Val Gly Lys Cys Pro Arg     530 535 540 Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala 545 550 555 560 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp                 565 570 575 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp             580 585 590 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp         595 600 605 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala     610 615 620 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala 625 630 635 640 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp                 645 650 655 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala             660 665 670 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu         675 680 685 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp     690 695 700 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly 705 710 715 720 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser                 725 730 735 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln             740 745 750 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn         755 760 765 Val Leu Ser Leu Leu Arg     770 <210> 228 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Perth / 16/2009 HA1-1L modified <400> 228 Glu Leu Val Gln Ser Ser Ser Thr Gly Glu Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Tyr Val         35 40 45 Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ala Cys Ile Arg Arg Ser Lys Asn Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr His Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Val Trp Gly Val His His     130 135 140 Pro Gly Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ala Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ser Pro Asn                 165 170 175 Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asp             260 265 270 Thr Leu Glu         275 <210> 229 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 IT214845 D3I-o1 <400> 229 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu         275 280 285 Gly Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser     290 295 300 Ala Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro 305 310 315 320 Gly Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser                 325 330 335 Gly Gly Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg             340 345 350 Thr Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr         355 360 365 Ala Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro     370 375 380 Gln Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile 385 390 395 400 Ile Trp Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu                 405 410 415 Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln             420 425 430 Gln Ser Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln         435 440 445 Ser Gly Arg Ile Asp Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr     450 455 460 Val Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser 465 470 475 480 Phe Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Ser Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 230 <211> 774 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 IT214845 D3I-o1 <400> 230 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Thr Val Glu Arg Thr Asn Val Pro Arg Ile Cys         275 280 285 Ser Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly     290 295 300 Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala 305 310 315 320 Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly                 325 330 335 Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly             340 345 350 Gly Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr         355 360 365 Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr Ala     370 375 380 Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln 385 390 395 400 Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile                 405 410 415 Trp Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr             420 425 430 Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln         435 440 445 Ser Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser     450 455 460 Gly Arg Ile Asp Phe His Trp Leu Met Leu Asn Pro Asn Asp Thr Val 465 470 475 480 Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe                 485 490 495 Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Ser Val Gln Val Asp Ala             500 505 510 Asn Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn         515 520 525 Leu Pro Phe Gln Asn Ile Asn Ser Arg Ala Val Gly Lys Cys Pro Arg     530 535 540 Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala 545 550 555 560 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp                 565 570 575 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp             580 585 590 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp         595 600 605 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala     610 615 620 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala 625 630 635 640 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp                 645 650 655 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala             660 665 670 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu         675 680 685 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp     690 695 700 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly 705 710 715 720 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser                 725 730 735 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln             740 745 750 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn         755 760 765 Val Leu Ser Leu Leu Arg     770 <210> 231 <211> 785 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L IT214845 D3I-o1 <400> 231 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Asn Ala Thr Glu Thr Val Glu Arg Thr Asn Val Pro         275 280 285 Arg Ile Cys Ser Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly     290 295 300 Leu Leu Gly Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu 305 310 315 320 Phe Ser Ala Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys                 325 330 335 Tyr Pro Gly Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg             340 345 350 Glu Ser Gly Gly Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly         355 360 365 Ile Arg Thr Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Gly Ser Ser     370 375 380 Phe Tyr Ala Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala 385 390 395 400 Phe Pro Gln Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala                 405 410 415 Leu Ile Ile Trp Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr             420 425 430 Lys Leu Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn         435 440 445 Tyr Gln Gln Ser Phe Val Ser Ser Pro Gly Ala Arg Pro Gln Val Asn     450 455 460 Gly Gln Ser Gly Arg Ile Asp Phe His Trp Leu Met Leu Asn Pro Asn 465 470 475 480 Asp Thr Val Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg                 485 490 495 Ala Ser Phe Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Ser Val Gln             500 505 510 Val Asp Ala Asn Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile         515 520 525 Ile Ser Asn Leu Pro Phe Gln Asn Ile Asn Ser Arg Ala Val Gly Lys     530 535 540 Cys Pro Arg Tyr Val Lys Gln Glu Ser Leu Met Leu Ala Thr Thr Lys 545 550 555 560 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp                 565 570 575 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn             580 585 590 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr         595 600 605 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala     610 615 620 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr 625 630 635 640 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly                 645 650 655 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn             660 665 670 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala         675 680 685 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala     690 695 700 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln 705 710 715 720 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn                 725 730 735 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu             740 745 750 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser         755 760 765 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu     770 775 780 Arg 785 <210> 232 <211> 711 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 NY107 D3I-o1 <400> 232 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu         275 280 285 Gly Thr Leu Ile Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser     290 295 300 Ser Asp Leu Ile Ile Glu Arg Arg Glu Gly Thr Asp Ile Cys Tyr Pro 305 310 315 320 Gly Arg Phe Thr Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg Arg Ser                 325 330 335 Gly Gly Ile Gly Lys Gly Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg             340 345 350 Thr Asn Gly Ala Thr Ser Ala Cys Thr Arg Ser Ser Ser Ser Phe Tyr         355 360 365 Ala Glu Met Lys Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala Phe Pro     370 375 380 Gln Met Thr Lys Ala Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile 385 390 395 400 Ile Trp Gly Val His His Ser Glu Ser Val Ser Glu Gln Thr Lys Leu                 405 410 415 Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Arg Ser Ser Lys Tyr Gln             420 425 430 Gln Ser Phe Thr Pro Asn Pro Gly Ala Arg Arg Ile Asp Phe His Trp         435 440 445 Leu Leu Leu Asp Pro Asn Asp Thr Val Thr Phe Thr Phe Asn Gly Ala     450 455 460 Phe Ile Ala Pro Asp Arg Thr Ser Phe Phe Arg Gly Glu Ser Leu Gly 465 470 475 480 Val Gln Ser Asp Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro                 485 490 495 Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val             500 505 510 Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr         515 520 525 Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly     530 535 540 Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys 545 550 555 560 Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala                 565 570 575 Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile             580 585 590 Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys         595 600 605 Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro     610 615 620 Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser 625 630 635 640 Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu                 645 650 655 Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp             660 665 670 Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu         675 680 685 Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln     690 695 700 Asn Val Leu Ser Leu Leu Arg 705 710 <210> 233 <211> 766 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 NY107 D3I-o1 <400> 233 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Thr Val Glu Thr Thr Asn Ile Lys Lys Ile Cys         275 280 285 Thr Gln Gly Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu Gly     290 295 300 Thr Leu Ile Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ser 305 310 315 320 Asp Leu Ile Ile Glu Arg Arg Glu Gly Thr Asp Ile Cys Tyr Pro Gly                 325 330 335 Arg Phe Thr Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg Arg Ser Gly             340 345 350 Gly Ile Gly Lys Glu Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr         355 360 365 Asn Gly Ala Thr Ser Ala Cys Thr Arg Ser Ser Ser Ser Phe Tyr Ala     370 375 380 Glu Met Lys Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala Phe Pro Gln 385 390 395 400 Met Thr Lys Ala Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile Ile                 405 410 415 Trp Gly Val His His Ser Glu Ser Val Ser Glu Gln Thr Lys Leu Tyr             420 425 430 Gly Ser Gly Asn Lys Leu Ile Thr Val Arg Ser Ser Lys Tyr Gln Gln         435 440 445 Ser Phe Thr Pro Asn Pro Gly Ala Arg Arg Ile Asp Phe His Trp Leu     450 455 460 Leu Leu Asp Pro Asn Asp Thr Val Thr Phe Thr Phe Asn Gly Ala Phe 465 470 475 480 Ile Ala Pro Asp Arg Thr Ser Phe Phe Arg Gly Glu Ser Leu Gly Val                 485 490 495 Gln Ser Asp Ala Pro Leu Asp Ser Ser Cys Arg Gly Asp Cys Phe His             500 505 510 Ser Gly Gly Thr Ile Val Ser Ser Leu Pro Phe Gln Asn Ile Asn Ser         515 520 525 Arg Thr Val Gly Lys Cys Pro Arg Tyr Val Lys Thr Lys Thr Glu Val     530 535 540 Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn 545 550 555 560 Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu                 565 570 575 Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly             580 585 590 Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp         595 600 605 Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala     610 615 620 Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly 625 630 635 640 Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys                 645 650 655 Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala             660 665 670 Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala         675 680 685 Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe     690 695 700 Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu 705 710 715 720 Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn                 725 730 735 Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala             740 745 750 Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg         755 760 765 <210> 234 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 NL12 D3I-O1 <400> 234 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu         275 280 285 Gly Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser     290 295 300 Ala Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro 305 310 315 320 Gly Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser                 325 330 335 Gly Gly Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg             340 345 350 Thr Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr         355 360 365 Ala Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro     370 375 380 Gln Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile 385 390 395 400 Ile Trp Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu                 405 410 415 Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln             420 425 430 Gln Ser Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln         435 440 445 Ser Gly Arg Ile Asp Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr     450 455 460 Val Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser 465 470 475 480 Phe Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Gly Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 235 <211> 774 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 NL12 D3I-o1 <400> 235 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Thr Val Glu Arg Thr Asn Val Pro Arg Ile Cys         275 280 285 Ser Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly     290 295 300 Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala 305 310 315 320 Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly                 325 330 335 Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly             340 345 350 Gly Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr         355 360 365 Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr Ala     370 375 380 Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln 385 390 395 400 Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile                 405 410 415 Trp Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr             420 425 430 Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln         435 440 445 Ser Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser     450 455 460 Gly Arg Ile Asp Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr Val 465 470 475 480 Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe                 485 490 495 Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Gly Val Gln Val Asp Ala             500 505 510 Asn Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn         515 520 525 Leu Pro Phe Gln Asn Ile Asn Ser Arg Ala Val Gly Lys Cys Pro Arg     530 535 540 Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala 545 550 555 560 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp                 565 570 575 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp             580 585 590 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp         595 600 605 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala     610 615 620 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala 625 630 635 640 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp                 645 650 655 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala             660 665 670 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu         675 680 685 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp     690 695 700 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly 705 710 715 720 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser                 725 730 735 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln             740 745 750 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn         755 760 765 Val Leu Ser Leu Leu Arg     770 <210> 236 <211> 785 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L NL12 D3I-o1 <400> 236 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Asn Ala Thr Glu Thr Val Glu Arg Thr Asn Val Pro         275 280 285 Arg Ile Cys Ser Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly     290 295 300 Leu Leu Gly Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu 305 310 315 320 Phe Ser Ala Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys                 325 330 335 Tyr Pro Gly Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg             340 345 350 Glu Ser Gly Gly Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly         355 360 365 Ile Arg Thr Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Gly Ser Ser     370 375 380 Phe Tyr Ala Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala 385 390 395 400 Phe Pro Gln Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala                 405 410 415 Leu Ile Ile Trp Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr             420 425 430 Lys Leu Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn         435 440 445 Tyr Gln Gln Ser Phe Val Ser Ser Pro Gly Ala Arg Pro Gln Val Asn     450 455 460 Gly Gln Ser Gly Arg Ile Asp Phe His Trp Leu Ile Leu Asn Pro Asn 465 470 475 480 Asp Thr Val Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg                 485 490 495 Ala Ser Phe Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Gly Val Gln             500 505 510 Val Asp Ala Asn Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile         515 520 525 Ile Ser Asn Leu Pro Phe Gln Asn Ile Asn Ser Arg Ala Val Gly Lys     530 535 540 Cys Pro Arg Tyr Val Lys Gln Glu Ser Leu Leu Leu Ala Thr Thr Lys 545 550 555 560 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp                 565 570 575 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn             580 585 590 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr         595 600 605 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala     610 615 620 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr 625 630 635 640 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly                 645 650 655 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn             660 665 670 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala         675 680 685 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala     690 695 700 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln 705 710 715 720 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn                 725 730 735 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu             740 745 750 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser         755 760 765 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu     770 775 780 Arg 785 <210> 237 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 CA504 D3I-o1 <400> 237 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu         275 280 285 Gly Thr Leu Ile Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Asp     290 295 300 Ala Asn Leu Ile Ile Glu Arg Arg Glu Gly Thr Asp Val Cys Tyr Pro 305 310 315 320 Gly Lys Phe Thr Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg Gly Ser                 325 330 335 Gly Gly Ile Asp Lys Glu Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg             340 345 350 Thr Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr         355 360 365 Ala Glu Met Lys Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala Phe Pro     370 375 380 Gln Met Thr Lys Ser Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile 385 390 395 400 Ile Trp Gly Val His His Ser Gly Ser Ala Thr Glu Gln Thr Lys Leu                 405 410 415 Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Lys Tyr Gln             420 425 430 Gln Ser Phe Thr Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln         435 440 445 Ser Gly Arg Ile Asp Phe His Trp Leu Leu Leu Asp Pro Asn Asp Thr     450 455 460 Val Thr Phe Thr Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser 465 470 475 480 Phe Phe Arg Gly Glu Ser Leu Gly Val Gln Ser Asp Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 238 <211> 774 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 CA504 D3I-o1 <400> 238 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Thr Val Glu Thr Val Asn Ile Lys Lys Ile Cys         275 280 285 Thr Gln Gly Lys Arg Pro Thr Asp Leu Gly Gln Cys Gly Leu Leu Gly     290 295 300 Thr Leu Ile Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Asp Ala 305 310 315 320 Asn Leu Ile Ile Glu Arg Arg Glu Gly Thr Asp Val Cys Tyr Pro Gly                 325 330 335 Lys Phe Thr Asn Glu Glu Ser Leu Arg Gln Ile Leu Arg Gly Ser Gly             340 345 350 Gly Ile Asp Lys Glu Ser Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr         355 360 365 Asn Gly Ala Thr Ser Ala Cys Arg Arg Ser Ser Ser Ser Phe Tyr Ala     370 375 380 Glu Met Lys Trp Leu Leu Ser Asn Ser Asp Asn Ala Ala Phe Pro Gln 385 390 395 400 Met Thr Lys Ser Tyr Arg Asn Pro Arg Asn Lys Pro Ala Leu Ile Ile                 405 410 415 Trp Gly Val His His Ser Gly Ser Ala Thr Glu Gln Thr Lys Leu Tyr             420 425 430 Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Lys Tyr Gln Gln         435 440 445 Ser Phe Thr Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser     450 455 460 Gly Arg Ile Asp Phe His Trp Leu Leu Leu Asp Pro Asn Asp Thr Val 465 470 475 480 Thr Phe Thr Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe                 485 490 495 Phe Arg Gly Glu Ser Leu Gly Val Gln Ser Ser Val Val Pro Leu Asp Ser             500 505 510 Gly Cys Glu Gly Asp Cys Phe His Ser Gly Gly Thr Ile Val Ser Ser         515 520 525 Leu Pro Phe Gln Asn Ile Asn Pro Arg Thr Val Gly Lys Cys Pro Arg     530 535 540 Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala 545 550 555 560 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp                 565 570 575 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp             580 585 590 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp         595 600 605 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala     610 615 620 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala 625 630 635 640 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp                 645 650 655 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala             660 665 670 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu         675 680 685 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp     690 695 700 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly 705 710 715 720 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser                 725 730 735 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln             740 745 750 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn         755 760 765 Val Leu Ser Leu Leu Arg     770 <210> 239 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 NL219 D3I-o1 <400> 239 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu         275 280 285 Gly Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser     290 295 300 Ala Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro 305 310 315 320 Gly Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser                 325 330 335 Gly Gly Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg             340 345 350 Thr Asn Gly Thr Thr Ser Ala Cys Arg Arg Ser Gly Ser Ser Phe Tyr         355 360 365 Ala Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro     370 375 380 Gln Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile 385 390 395 400 Ile Trp Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu                 405 410 415 Tyr Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln             420 425 430 Gln Ser Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln         435 440 445 Ser Gly Arg Ile Asp Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr     450 455 460 Val Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser 465 470 475 480 Phe Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Glu Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 240 <211> 774 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 NL219 D3I-o1 <400> 240 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Thr Val Glu Arg Thr Asn Val Pro Arg Ile Cys         275 280 285 Ser Lys Gly Lys Arg Thr Val Asp Leu Gly Gln Cys Gly Leu Leu Gly     290 295 300 Thr Ile Thr Gly Pro Pro Gln Cys Asp Gln Phe Leu Glu Phe Ser Ala 305 310 315 320 Asp Leu Ile Ile Glu Arg Arg Glu Gly Ser Asp Val Cys Tyr Pro Gly                 325 330 335 Lys Phe Val Asn Glu Glu Ala Leu Arg Gln Ile Leu Arg Glu Ser Gly             340 345 350 Gly Ile Asp Lys Glu Thr Met Gly Phe Thr Tyr Ser Gly Ile Arg Thr         355 360 365 Asn Gly Thr Ser Ser Ala Cys Arg Ser Ser Gly Ser Ser Phe Tyr Ala     370 375 380 Glu Met Lys Trp Leu Leu Ser Asn Thr Asp Asn Ala Ala Phe Pro Gln 385 390 395 400 Met Thr Lys Ser Tyr Lys Asn Thr Arg Lys Asp Pro Ala Leu Ile Ile                 405 410 415 Trp Gly Ile His His Ser Gly Ser Thr Thr Glu Gln Thr Lys Leu Tyr             420 425 430 Gly Ser Gly Asn Lys Leu Ile Thr Val Gly Ser Ser Asn Tyr Gln Gln         435 440 445 Ser Phe Val Pro Ser Pro Gly Ala Arg Pro Gln Val Asn Gly Gln Ser     450 455 460 Gly Arg Ile Asp Phe His Trp Leu Ile Leu Asn Pro Asn Asp Thr Val 465 470 475 480 Thr Phe Ser Phe Asn Gly Ala Phe Ile Ala Pro Asp Arg Ala Ser Phe                 485 490 495 Leu Arg Gly Lys Ser Met Gly Ile Gln Ser Glu Val Gln Val Asp Ala             500 505 510 Asn Cys Glu Gly Asp Cys Tyr His Ser Gly Gly Thr Ile Ile Ser Asn         515 520 525 Leu Pro Phe Gln Asn Ile Asn Ser Arg Ala Val Gly Lys Cys Pro Arg     530 535 540 Tyr Val Lys Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala 545 550 555 560 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp                 565 570 575 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp             580 585 590 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp         595 600 605 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala     610 615 620 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala 625 630 635 640 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp                 645 650 655 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala             660 665 670 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu         675 680 685 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp     690 695 700 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly 705 710 715 720 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser                 725 730 735 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln             740 745 750 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn         755 760 765 Val Leu Ser Leu Leu Arg     770 <210> 241 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 HK33982 D3I-o1 <400> 241 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu         275 280 285 Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Glu Gly Arg     290 295 300 Glu Trp Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Thr Cys 305 310 315 320 Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Thr Leu Phe Ser                 325 330 335 Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Thr Trp             340 345 350 Asn Val Thr Tyr Thr Gly Thr Ser Arg Ser Cys Ser Gly Ser Phe Tyr         355 360 365 Arg Ser Met Arg Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro Val Gln     370 375 380 Asp Ala Lys Tyr Thr Asn Asn Arg Gly Lys Asn Ile Leu Phe Val Trp 385 390 395 400 Gly Ile His His Pro His Thr Tyr Thr Asp Gln Thr Thr Leu Tyr Ile                 405 410 415 Arg Asn Asp Thr Thr Thr Ser Val Thr Thr Glu Glu Leu Asn Arg Ile             420 425 430 Phe Lys Pro Val Ile Val Pro Arg Leu Leu Val Asn Gly Gln Gln Gly         435 440 445 Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg     450 455 460 Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Val Leu 465 470 475 480 Ser Gly Gly Ser Gly Arg Ile Leu Lys Thr Asp Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 242 <211> 771 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 HK33982 D3I-o1 <400> 242 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gln Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn         275 280 285 Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile     290 295 300 Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Glu Gly Arg Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Thr Cys Tyr Pro Gly                 325 330 335 Asn Val Glu Asn Leu Glu Glu Leu Arg Thr Leu Phe Ser Ser Ala Ser             340 345 350 Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Thr Trp Asn Val Thr         355 360 365 Tyr Thr Gly Thr Ser Arg Ser Cys Ser Gly Ser Phe Tyr Arg Ser Met     370 375 380 Arg Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro Val Gln Asp Ala Lys 385 390 395 400 Tyr Thr Asn Asn Arg Gly Lys Asn Ile Leu Phe Val Trp Gly Ile His                 405 410 415 His Pro His Thr Tyr Thr Asp Gln Thr Thr Leu Tyr Ile Arg Asn Asp             420 425 430 Thr Thr Ser Val Thr Thr Glu Glu Leu Asn Arg Ile Phe Lys Pro         435 440 445 Val Ile Val Pro Arg Leu Leu Val Asn Gly Gln Gln Gly Arg Ile Asp     450 455 460 Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Arg Ser 465 470 475 480 Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Val Leu Ser Gly Gly                 485 490 495 Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys Ser Gly Asn Cys Val             500 505 510 Val Gln Cys Gln Thr Glu Lys Gly Gly Leu Asn Ser Thr Leu Pro Phe         515 520 525 His Asn Ile Ser Lys Tyr Ala Phe Gly Thr Cys Pro Lys Tyr Val Lys     530 535 540 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser 545 550 555 560 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp                 565 570 575 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly             580 585 590 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr         595 600 605 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr     610 615 620 Ser Tyr Thr Ala Asp Asp Gly Thr 625 630 635 640 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr                 645 650 655 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu             660 665 670 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile         675 680 685 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala     690 695 700 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val 705 710 715 720 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala                 725 730 735 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly             740 745 750 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser         755 760 765 Leu Leu Arg     770 <210> 243 <211> 783 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L HK33982 D3I-o1 <400> 243 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ala Lys Glu Leu Leu Gln Thr Glu His Asn Gly Met         275 280 285 Leu Cys Ala Thr Asn Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr     290 295 300 Ile Glu Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Glu 305 310 315 320 Gly Arg Glu Trp Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly                 325 330 335 Thr Cys Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Thr Leu             340 345 350 Phe Ser Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr         355 360 365 Thr Trp Asn Val Thr Tyr Thr Gly Thr Ser Arg Ser Ser Cys Ser Gly Ser     370 375 380 Phe Tyr Arg Ser Met Arg Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro 385 390 395 400 Val Gln Asp Ala Lys Tyr Thr Asn Asn Arg Gly Lys Asn Ile Leu Phe                 405 410 415 Val Trp Gly Ile His His His Thr Tyr Thr Asp Gln Thr Thr Leu             420 425 430 Tyr Ile Arg Asn Asp Thr Thr Thr Ser Val Thr Thr Glu Glu Leu Asn         435 440 445 Arg Ile Phe Lys Pro Val Ile Val Pro Arg Leu Leu Val Asn Gly Gln     450 455 460 Gln Gly Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr 465 470 475 480 Leu Arg Val Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His                 485 490 495 Val Leu Ser Gly Gly Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys             500 505 510 Ser Gly Asn Cys Val Val Gln Cys Gln Thr Glu Lys Gly Gly Leu Asn         515 520 525 Ser Thr Leu Pro Phe His Asn Ile Ser Lys Tyr Ala Phe Gly Thr Cys     530 535 540 Pro Lys Tyr Val Lys Val Asn Ser Leu Lys Leu Ala Thr Lys Thr Glu 545 550 555 560 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys                 565 570 575 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala             580 585 590 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu         595 600 605 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr     610 615 620 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala 625 630 635 640 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp                 645 650 655 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser             660 665 670 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala         675 680 685 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu     690 695 700 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg 705 710 715 720 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser                 725 730 735 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser             740 745 750 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu         755 760 765 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 780 <210> 244 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 HK1073 D3I-o1 <400> 244 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu         275 280 285 Gly Leu Val Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg     290 295 300 Glu Trp Ser Tyr Ile Val Glu Arg Ser Ser Ala Val Asn Gly Thr Cys 305 310 315 320 Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Thr Leu Phe Ser                 325 330 335 Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Thr Trp             340 345 350 Asn Val Thr Tyr Thr Gly Thr Ser Arg Ala Cys Ser Gly Ser Phe Tyr         355 360 365 Arg Ser Met Arg Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro Val Gln     370 375 380 Asp Ala Gln Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Val Trp 385 390 395 400 Gly Ile His His Pro Pro Thr Tyr Thr Glu Gln Thr Asn Leu Tyr Ile                 405 410 415 Arg Asn Asp Thr Thr Thr Ser Val Thr Thr Glu Asp Leu Asn Arg Thr             420 425 430 Phe Lys Pro Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly         435 440 445 Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg     450 455 460 Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Val Leu 465 470 475 480 Ser Gly Gly Ser Gly Arg Ile Leu Lys Thr Asp Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 245 <211> 771 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 HK1073 D3I-o1 <400> 245 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Thr Glu His Asn Gly Met Leu Cys Ala Thr Ser         275 280 285 Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Val     290 295 300 Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Arg Ser Ser Ala Val Asn Gly Thr Cys Tyr Pro Gly                 325 330 335 Asn Val Glu Asn Leu Glu Glu Leu Arg Thr Leu Phe Ser Ser Ala Ser             340 345 350 Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Thr Trp Asn Val Thr         355 360 365 Tyr Thr Gly Thr Ser Arg Ala Cys Ser Gly Ser Phe Tyr Arg Ser Met     370 375 380 Arg Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro Val Gln Asp Ala Gln 385 390 395 400 Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Val Trp Gly Ile His                 405 410 415 His Pro Pro Thr Tyr Thr Glu Gln Thr Asn Leu Tyr Ile Arg Asn Asp             420 425 430 Thr Thr Thr Ser Val Thr Thr Glu Asp Leu Asn Arg Thr Phe Lys Pro         435 440 445 Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile Asp     450 455 460 Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Arg Ser 465 470 475 480 Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Val Leu Ser Gly Gly                 485 490 495 Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys Gly Gly Asn Cys Val             500 505 510 Val Gln Cys Gln Thr Glu Lys Gly Gly Leu Asn Ser Thr Leu Pro Phe         515 520 525 His Asn Ile Ser Lys Tyr Ala Phe Gly Thr Cys Pro Lys Tyr Val Arg     530 535 540 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser 545 550 555 560 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp                 565 570 575 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly             580 585 590 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr         595 600 605 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr     610 615 620 Ser Tyr Thr Ala Asp Asp Gly Thr 625 630 635 640 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr                 645 650 655 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu             660 665 670 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile         675 680 685 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala     690 695 700 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val 705 710 715 720 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala                 725 730 735 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly             740 745 750 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser         755 760 765 Leu Leu Arg     770 <210> 246 <211> 783 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L HK1073 D3I-o1 <400> 246 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met         275 280 285 Leu Cys Ala Thr Ser Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr     290 295 300 Ile Glu Gly Leu Val Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly 305 310 315 320 Gly Arg Glu Trp Ser Tyr Ile Val Glu Arg Ser Ser Ala Val Asn Gly                 325 330 335 Thr Cys Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Thr Leu             340 345 350 Phe Ser Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr         355 360 365 Thr Trp Asn Val Thr Tyr Thr Gly Thr Ser Arg Ala Cys Ser Gly Ser     370 375 380 Phe Tyr Arg Ser Met Arg Trp Leu Thr Gln Lys Ser Gly Phe Tyr Pro 385 390 395 400 Val Gln Asp Ala Gln Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe                 405 410 415 Val Trp Gly Ile His His Pro Pro Thr Tyr Thr Glu Gln Thr Asn Leu             420 425 430 Tyr Ile Arg Asn Asp Thr Thr Thr Ser Val Thr Thr Glu Asp Leu Asn         435 440 445 Arg Thr Phe Lys Pro Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu     450 455 460 Gln Gly Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr 465 470 475 480 Leu Arg Val Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His                 485 490 495 Val Leu Ser Gly Gly Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys             500 505 510 Gly Asn Cys Val Val Gln Cys Gln Thr Glu Lys Gly Gly Leu Asn         515 520 525 Ser Thr Leu Pro Phe His Asn Ile Ser Lys Tyr Ala Phe Gly Thr Cys     530 535 540 Pro Lys Tyr Val Arg Val Asn Ser Leu Lys Leu Ala Thr Lys Thr Glu 545 550 555 560 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys                 565 570 575 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala             580 585 590 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu         595 600 605 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr     610 615 620 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala 625 630 635 640 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp                 645 650 655 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser             660 665 670 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala         675 680 685 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu     690 695 700 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg 705 710 715 720 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser                 725 730 735 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser             740 745 750 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu         755 760 765 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 780 <210> 247 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 HKG9 D3I-o1 <400> 247 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu         275 280 285 Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg     290 295 300 Glu Trp Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Met Cys 305 310 315 320 Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Phe Phe Ser                 325 330 335 Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp             340 345 350 Asn Val Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr         355 360 365 Arg Ser Met Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln     370 375 380 Asp Ala Gln Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Met Trp 385 390 395 400 Gly Ile Asn His Pro Pro Thr Asp Thr Ala Gln Thr Asn Leu Tyr Thr                 405 410 415 Arg Thr Asp Thr Thr Thr Ser Val Ala Thr Glu Asp Ile Asn Arg Thr             420 425 430 Phe Lys Pro Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly         435 440 445 Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg     450 455 460 Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu 465 470 475 480 Ser Gly Glu Ser Gly Arg Ile Leu Lys Thr Asp Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 248 <211> 771 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 HKG9 D3I-o1 <400> 248 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn         275 280 285 Leu Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile     290 295 300 Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Met Cys Tyr Pro Gly                 325 330 335 Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Phe Phe Ser Ser Ala Ser             340 345 350 Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser         355 360 365 Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Met     370 375 380 Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala Gln 385 390 395 400 Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Met Trp Gly Ile Asn                 405 410 415 His Pro Thr Asp Thr Ala Gln Thr Asn Leu Tyr Thr Arg Thr Asp             420 425 430 Thr Thr Thr Ser Ala Thr Glu Asp Ile Asn Arg Thr Phe Lys Pro         435 440 445 Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile Asp     450 455 460 Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Arg Ser 465 470 475 480 Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu                 485 490 495 Ser His Gly Arg Ile Leu Lys Thr Asp Leu Asn Ser Gly Ser Cys Val             500 505 510 Val Gln Cys Gln Thr Glu Arg Gly Gly Leu Asn Thr Thr Leu Pro Phe         515 520 525 His Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys Pro Lys Tyr Val Gly     530 535 540 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser 545 550 555 560 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp                 565 570 575 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly             580 585 590 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr         595 600 605 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr     610 615 620 Ser Tyr Thr Ala Asp Asp Gly Thr 625 630 635 640 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr                 645 650 655 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu             660 665 670 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile         675 680 685 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala     690 695 700 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val 705 710 715 720 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala                 725 730 735 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly             740 745 750 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser         755 760 765 Leu Leu Arg     770 <210> 249 <211> 783 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L HKG9 D3I-o1 <400> 249 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met         275 280 285 Leu Cys Ala Thr Asn Leu Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr     290 295 300 Ile Glu Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly 305 310 315 320 Gly Arg Glu Trp Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly                 325 330 335 Met Cys Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Phe             340 345 350 Phe Ser Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr         355 360 365 Ile Trp Asn Val Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser     370 375 380 Phe Tyr Arg Ser Met Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro 385 390 395 400 Ile Gln Asp Ala Gln Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe                 405 410 415 Met Trp Gly Ile Asn His Pro Pro Thr Asp Thr Ala Gln Thr Asn Leu             420 425 430 Tyr Thr Arg Thr Asp Thr Thr Thr Ser Val Ala Thr Glu Asp Ile Asn         435 440 445 Arg Thr Phe Lys Pro Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu     450 455 460 Gln Gly Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr 465 470 475 480 Leu Arg Val Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His                 485 490 495 Ile Leu Ser Gly Glu Ser His Gly Arg Ile Leu Lys Thr Asp Leu Asn             500 505 510 Ser Gly Ser Cys Val Val Gln Cys Gln Thr Glu Arg Gly Gly Leu Asn         515 520 525 Thr Thr Leu Pro Phe His Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys     530 535 540 Pro Lys Tyr Val Gly Val Lys Ser Leu Lys Leu Ala Thr Lys Thr Glu 545 550 555 560 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys                 565 570 575 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala             580 585 590 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu         595 600 605 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr     610 615 620 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala 625 630 635 640 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp                 645 650 655 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser             660 665 670 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala         675 680 685 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu     690 695 700 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg 705 710 715 720 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser                 725 730 735 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser             740 745 750 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu         755 760 765 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 780 <210> 250 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 AH16 D3I-o1 <400> 250 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu         275 280 285 Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Gly     290 295 300 Glu Trp Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Leu Cys 305 310 315 320 Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser                 325 330 335 Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp             340 345 350 Asn Val Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr         355 360 365 Arg Ser Met Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln     370 375 380 Asp Ala Gln Tyr Thr Asn Asn Arg Glu Lys Asn Ile Leu Phe Met Trp 385 390 395 400 Gly Ile Asn Gln Pro Pro Thr Glu Thr Ala Gln Thr Asn Leu Tyr Thr                 405 410 415 Arg Thr Asp Thr Thr Thr Ser Val Ala Thr Glu Glu Ile Asn Arg Thr             420 425 430 Phe Lys Pro Leu Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly         435 440 445 Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg     450 455 460 Ile Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu 465 470 475 480 Ser Gly Glu Ser Gly Arg Ile Leu Lys Thr Asp Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 251 <211> 771 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 AH16 D3I-o1 <400> 251 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn         275 280 285 Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile     290 295 300 Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Gly Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Leu Cys Tyr Pro Gly                 325 330 335 Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ala Ser             340 345 350 Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser         355 360 365 Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Met     370 375 380 Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala Gln 385 390 395 400 Tyr Thr Asn Asn Arg Glu Lys Asn Ile Leu Phe Met Trp Gly Ile Asn                 405 410 415 Gln Pro Pro Thr Glu Thr Ala Gln Thr Asn Leu Tyr Thr Arg Thr Asp             420 425 430 Thr Thr Ser Val Ala Thr Glu Glu Ile Asn Arg Thr Phe Lys Pro         435 440 445 Leu Ile Gly Pro Arg Pro Leu Val Asn Gly Leu Gln Gly Arg Ile Asp     450 455 460 Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Ile Arg Ser 465 470 475 480 Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu                 485 490 495 Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys Arg Gly Ser Cys Thr             500 505 510 Val Gln Cys Gln Thr Glu Lys Gly Gly Leu Asn Thr Thr Leu Pro Phe         515 520 525 Gln Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys Ser Lys Tyr Val Gly     530 535 540 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser 545 550 555 560 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp                 565 570 575 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly             580 585 590 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr         595 600 605 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr     610 615 620 Ser Tyr Thr Ala Asp Asp Gly Thr 625 630 635 640 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr                 645 650 655 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu             660 665 670 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile         675 680 685 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala     690 695 700 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val 705 710 715 720 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala                 725 730 735 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly             740 745 750 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser         755 760 765 Leu Leu Arg     770 <210> 252 <211> 783 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L AH16 D3I-o1 <400> 252 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met         275 280 285 Leu Cys Ala Thr Asn Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr     290 295 300 Ile Glu Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly 305 310 315 320 Gly Gly Glu Trp Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly                 325 330 335 Leu Cys Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu             340 345 350 Phe Ser Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr         355 360 365 Ile Trp Asn Val Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser     370 375 380 Phe Tyr Arg Ser Met Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro 385 390 395 400 Ile Gln Asp Ala Gln Tyr Thr Asn Asn Arg Glu Lys Asn Ile Leu Phe                 405 410 415 Met Trp Gly Ile Asn Gln Pro Pro Thr Glu Thr Ala Gln Thr Asn Leu             420 425 430 Tyr Thr Arg Thr Asp Thr Thr Thr Ser Val Ala Thr Glu Glu Ile Asn         435 440 445 Arg Thr Phe Lys Pro Leu Ile Gly Pro Arg Pro Leu Val Asn Gly Leu     450 455 460 Gln Gly Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr 465 470 475 480 Leu Arg Ile Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His                 485 490 495 Ile Leu Ser Gly Glu Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys             500 505 510 Arg Gly Ser Cys Thr Val Gln Cys Gln Thr Glu Lys Gly Gly Leu Asn         515 520 525 Thr Thr Leu Pro Phe Gln Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys     530 535 540 Ser Lys Tyr Val Gly Ile Lys Ser Leu Lys Leu Ala Thr Lys Thr Glu 545 550 555 560 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys                 565 570 575 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala             580 585 590 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu         595 600 605 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr     610 615 620 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala 625 630 635 640 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp                 645 650 655 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser             660 665 670 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala         675 680 685 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu     690 695 700 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg 705 710 715 720 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser                 725 730 735 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser             740 745 750 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu         755 760 765 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 780 <210> 253 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 HK9 D3I-o1 <400> 253 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu         275 280 285 Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg     290 295 300 Glu Trp Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Met Cys 305 310 315 320 Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser                 325 330 335 Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp             340 345 350 Asn Val Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr         355 360 365 Arg Ser Met Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln     370 375 380 Asp Ala Gln Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Met Trp 385 390 395 400 Gly Ile Asn His Pro Thr Asp Thr Val Gln Thr Asn Leu Tyr Thr                 405 410 415 Arg Thr Asp Thr Thr Thr Ser Val Thr Thr Glu Asp Ile Asn Arg Thr             420 425 430 Phe Lys Pro Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu His Gly         435 440 445 Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg     450 455 460 Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu 465 470 475 480 Ser Gly Glu Ser Gly Arg Ile Leu Lys Thr Asp Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 254 <211> 771 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 HK9 D3I-o1 <400> 254 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn         275 280 285 Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile     290 295 300 Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly Met Cys Tyr Pro Gly                 325 330 335 Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ala Ser             340 345 350 Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser         355 360 365 Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Met     370 375 380 Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro Ile Gln Asp Ala Gln 385 390 395 400 Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe Met Trp Gly Ile Asn                 405 410 415 His Pro Thr Asp Thr Val Gln Thr Asn Leu Tyr Thr Arg Thr Asp             420 425 430 Thr Thr Thr Ser Thr Thr Glu Asp Ile Asn Arg Thr Phe Lys Pro         435 440 445 Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu His Gly Arg Ile Asp     450 455 460 Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr Leu Arg Val Arg Ser 465 470 475 480 Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu                 485 490 495 Ser His Gly Arg Ile Leu Lys Thr Asp Leu Asn Ser Gly Asn Cys Val             500 505 510 Val Gln Cys Gln Thr Glu Arg Gly Gly Leu Asn Thr Thr Leu Pro Phe         515 520 525 His Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys Pro Lys Tyr Val Gly     530 535 540 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser 545 550 555 560 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp                 565 570 575 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly             580 585 590 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr         595 600 605 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr     610 615 620 Ser Tyr Thr Ala Asp Asp Gly Thr 625 630 635 640 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr                 645 650 655 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu             660 665 670 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile         675 680 685 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala     690 695 700 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val 705 710 715 720 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala                 725 730 735 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly             740 745 750 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser         755 760 765 Leu Leu Arg     770 <210> 255 <211> 783 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L HK9 D3I-o1 <400> 255 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met         275 280 285 Leu Cys Ala Thr Asn Leu Gly His Pro Leu Ile Leu Asp Thr Cys Thr     290 295 300 Ile Glu Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly 305 310 315 320 Gly Arg Glu Trp Ser Tyr Ile Val Glu Arg Pro Ser Ala Val Asn Gly                 325 330 335 Met Cys Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu             340 345 350 Phe Ser Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr         355 360 365 Ile Trp Asn Val Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser     370 375 380 Phe Tyr Arg Ser Met Arg Trp Leu Thr Gln Lys Asn Asn Ala Tyr Pro 385 390 395 400 Ile Gln Asp Ala Gln Tyr Thr Asn Asn Arg Gly Lys Ser Ile Leu Phe                 405 410 415 Met Trp Gly Ile Asn His Pro Pro Thr Asp Thr Val Gln Thr Asn Leu             420 425 430 Tyr Thr Arg Thr Asp Thr Thr Thr Ser Val Thr Thr Glu Asp Ile Asn         435 440 445 Arg Thr Phe Lys Pro Val Ile Gly Pro Arg Pro Leu Val Asn Gly Leu     450 455 460 His Gly Arg Ile Asp Tyr Tyr Trp Ser Val Leu Lys Pro Gly Gln Thr 465 470 475 480 Leu Arg Val Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His                 485 490 495 Ile Leu Ser Gly Glu Ser His Gly Arg Ile Leu Lys Thr Asp Leu Asn             500 505 510 Ser Gly Asn Cys Val Val Gln Cys Gln Thr Glu Arg Gly Gly Leu Asn         515 520 525 Thr Thr Leu Pro Phe His Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys     530 535 540 Pro Lys Tyr Val Gly Val Lys Ser Leu Lys Leu Ala Thr Lys Thr Glu 545 550 555 560 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys                 565 570 575 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala             580 585 590 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu         595 600 605 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr     610 615 620 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala 625 630 635 640 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp                 645 650 655 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser             660 665 670 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala         675 680 685 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu     690 695 700 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg 705 710 715 720 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser                 725 730 735 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser             740 745 750 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu         755 760 765 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 780 <210> 256 <211> 719 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 GX58 D3I-o1 <400> 256 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu         275 280 285 Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg     290 295 300 Glu Trp Ser Tyr Ile Val Glu Arg Ser Ser Ala Val Asn Gly Met Cys 305 310 315 320 Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser                 325 330 335 Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp             340 345 350 Asn Val Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr         355 360 365 Arg Ser Met Arg Trp Leu Thr Gln Lys Asp Asn Ala Tyr Pro Ile Gln     370 375 380 Asp Ala Gln Tyr Thr Asn Asn Arg Gly Arg Ser Ile Leu Phe Met Trp 385 390 395 400 Gly Ile Asn His Pro Pro Thr Asp Thr Thr Gln Thr Asn Leu Tyr Thr                 405 410 415 Arg Thr Asp Thr Thr Thr Ser Val Ala Thr Glu Asp Ile Asn Arg Thr             420 425 430 Phe Lys Pro Leu Ile Gly Pro Arg Pro Leu Val Asn Gly Gln Gln Gly         435 440 445 Arg Ile Asp Tyr Tyr Trp Ser Ile Leu Lys Pro Gly Gln Thr Leu Arg     450 455 460 Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu 465 470 475 480 Ser Gly Glu Ser Gly Arg Ile Leu Lys Thr Asp Thr Lys Thr Glu                 485 490 495 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys             500 505 510 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala         515 520 525 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu     530 535 540 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr 545 550 555 560 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala                 565 570 575 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp             580 585 590 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser         595 600 605 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala     610 615 620 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu 625 630 635 640 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg                 645 650 655 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser             660 665 670 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser         675 680 685 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu     690 695 700 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg 705 710 715 <210> 257 <211> 771 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1 GX58 D3I-o1 <400> 257 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala His Thr Glu His Asn Gly Met Leu Cys Ala Thr Asn         275 280 285 Leu Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr Ile Glu Gly Leu Ile     290 295 300 Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly Gly Arg Glu Trp Ser 305 310 315 320 Tyr Ile Val Glu Arg Ser Ser Ala Val Asn Gly Met Cys Tyr Pro Gly                 325 330 335 Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu Phe Ser Ser Ala Ser             340 345 350 Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr Ile Trp Asn Val Ser         355 360 365 Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser Phe Tyr Arg Ser Met     370 375 380 Arg Trp Leu Thr Gln Lys Asp Asn Ala Tyr Pro Ile Gln Asp Ala Gln 385 390 395 400 Tyr Thr Asn Asn Arg Gly Arg Ser Ile Leu Phe Met Trp Gly Ile Asn                 405 410 415 His Pro Thr Asp Thr Thr Gln Thr Asn Leu Tyr Thr Arg Thr Asp             420 425 430 Thr Thr Thr Ser Ala Thr Glu Asp Ile Asn Arg Thr Phe Lys Pro         435 440 445 Leu Ile Gly Pro Arg Pro Leu Val Asn Gly Gln Gln Gly Arg Ile Asp     450 455 460 Tyr Tyr Trp Ser Ile Leu Lys Pro Gly Gln Thr Leu Arg Val Arg Ser 465 470 475 480 Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His Ile Leu Ser Gly Glu                 485 490 495 Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys Lys Gly Asn Cys Val             500 505 510 Val Gln Cys Gln Thr Glu Arg Gly Gly Leu Asn Thr Thr Leu Pro Phe         515 520 525 His Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys Pro Lys Tyr Ile Gly     530 535 540 Thr Lys Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser 545 550 555 560 Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp                 565 570 575 Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly             580 585 590 Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr         595 600 605 Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr     610 615 620 Ser Tyr Thr Ala Asp Asp Gly Thr 625 630 635 640 Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr                 645 650 655 Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu             660 665 670 Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile         675 680 685 Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala     690 695 700 Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val 705 710 715 720 Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala                 725 730 735 Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly             740 745 750 Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser         755 760 765 Leu Leu Arg     770 <210> 258 <211> 783 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L GX58 D3I-o1 <400> 258 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Ala Lys Glu Leu Leu His Thr Glu His Asn Gly Met         275 280 285 Leu Cys Ala Thr Asn Leu Gly Arg Pro Leu Ile Leu Asp Thr Cys Thr     290 295 300 Ile Glu Gly Leu Ile Tyr Gly Asn Pro Ser Cys Asp Leu Leu Leu Gly 305 310 315 320 Gly Arg Glu Trp Ser Tyr Ile Val Glu Arg Ser Ser Ala Val Asn Gly                 325 330 335 Met Cys Tyr Pro Gly Asn Val Glu Asn Leu Glu Glu Leu Arg Ser Leu             340 345 350 Phe Ser Ser Ala Ser Ser Tyr Gln Arg Ile Gln Ile Phe Pro Asp Thr         355 360 365 Ile Trp Asn Val Ser Tyr Ser Gly Thr Ser Lys Ala Cys Ser Asp Ser     370 375 380 Phe Tyr Arg Ser Met Arg Trp Leu Thr Gln Lys Asp Asn Ala Tyr Pro 385 390 395 400 Ile Gln Asp Ala Gln Tyr Thr Asn Asn Arg Gly Arg Ser Ile Leu Phe                 405 410 415 Met Trp Gly Ile Asn His Pro Pro Thr Asp Thr Thr Gln Thr Asn Leu             420 425 430 Tyr Thr Arg Thr Asp Thr Thr Thr Ser Val Ala Thr Glu Asp Ile Asn         435 440 445 Arg Thr Phe Lys Pro Leu Ile Gly Pro Arg Pro Leu Val Asn Gly Gln     450 455 460 Gln Gly Arg Ile Asp Tyr Tyr Trp Ser Ile Leu Lys Pro Gly Gln Thr 465 470 475 480 Leu Arg Val Val Arg Ser Asn Gly Asn Leu Ile Ala Pro Trp Tyr Gly His                 485 490 495 Ile Leu Ser Gly Glu Ser His Gly Arg Ile Leu Lys Thr Asp Leu Lys             500 505 510 Lys Gly Asn Cys Val Val Gln Cys Gln Thr Glu Arg Gly Gly Leu Asn         515 520 525 Thr Thr Leu Pro Phe His Asn Val Ser Lys Tyr Ala Phe Gly Asn Cys     530 535 540 Pro Lys Tyr Ile Gly Val Lys Ser Leu Lys Leu Ala Thr Lys Thr Glu 545 550 555 560 Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys                 565 570 575 Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala             580 585 590 Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu         595 600 605 Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr     610 615 620 Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala 625 630 635 640 Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp                 645 650 655 Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser             660 665 670 Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala         675 680 685 Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu     690 695 700 Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg 705 710 715 720 Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser                 725 730 735 Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser             740 745 750 Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu         755 760 765 Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 780 <210> 259 <211> 752 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 D3I-o1 with extension <400> 259 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys     290 295 300 Val Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser             340 345 350 Thr Gln Asn Val Ile Asp Ala Glu Lys Ala Leu Gly Gly Pro Tyr Arg         355 360 365 Leu Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Asn Lys Asn Ala 385 390 395 400 Thr Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu                 405 410 415 Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met             420 425 430 Lys Asn Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala         435 440 445 Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asp     450 455 460 Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp 465 470 475 480 Tyr Met Val Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg                 485 490 495 Gly Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser             500 505 510 Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys Thr         515 520 525 Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp Ala     530 535 540 Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn Gly 545 550 555 560 Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile                 565 570 575 Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp             580 585 590 Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr         595 600 605 Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly Val     610 615 620 Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala 625 630 635 640 Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu                 645 650 655 Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala             660 665 670 Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln Asn         675 680 685 Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn Leu     690 695 700 Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val 705 710 715 720 Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser Val                 725 730 735 Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu Arg             740 745 750 <210> 260 <211> 753 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 D3I-o1 with extension <400> 260 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys     290 295 300 Thr Gly Asn Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser             340 345 350 Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Ser Tyr Lys         355 360 365 Ile Gly Thr Ser Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Asn Asn Lys Thr 385 390 395 400 Ala Thr Asn Ser Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly                 405 410 415 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu Ala Gln             420 425 430 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser         435 440 445 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro     450 455 460 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val 465 470 475 480 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln                 485 490 495 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser             500 505 510 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys         515 520 525 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp     530 535 540 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn 545 550 555 560 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr                 565 570 575 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala             580 585 590 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr         595 600 605 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly     610 615 620 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn 625 630 635 640 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala                 645 650 655 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala             660 665 670 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln         675 680 685 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn     690 695 700 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu 705 710 715 720 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser                 725 730 735 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu             740 745 750 Arg      <210> 261 <211> 753 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 D3I-o1 with extension <400> 261 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Lys         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys     290 295 300 Thr Gly Asn Ile Pro Ser Ala Glu Val Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg Leu Ser             340 345 350 Thr His Asn Val Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Lys         355 360 365 Ile Gly Thr Ser Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Asn Asn Lys Thr 385 390 395 400 Ala Thr Asn Ser Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly                 405 410 415 Glu Asp Gln Ile Thr Ile Trp Gly Phe His Ser Asp Ser Glu Thr Gln             420 425 430 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser         435 440 445 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro     450 455 460 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val 465 470 475 480 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln                 485 490 495 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser             500 505 510 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys         515 520 525 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp     530 535 540 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn 545 550 555 560 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr                 565 570 575 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala             580 585 590 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr         595 600 605 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly     610 615 620 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn 625 630 635 640 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala                 645 650 655 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala             660 665 670 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln         675 680 685 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn     690 695 700 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu 705 710 715 720 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser                 725 730 735 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu             740 745 750 Arg      <210> 262 <211> 753 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-2 D3I-o1 with extension <400> 262 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Lys Gly Thr Lys Thr Arg Gly Lys Leu Cys Pro Lys         275 280 285 Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Lys Cys     290 295 300 Thr Gly Asn Ile Pro Ser Ala Lys Val Ser Ile Leu His Glu Val Arg 305 310 315 320 Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile                 325 330 335 Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Arg Ile Arg Leu Ser             340 345 350 Asn His Asn Val Ile Asn Ala Glu Lys Ala Pro Gly Gly Pro Tyr Lys         355 360 365 Ile Gly Thr Ser Gly Ser Cys Pro Asn Val Thr Asn Gly Asn Gly Phe     370 375 380 Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Glu Asn Asn Lys Thr 385 390 395 400 Ala Thr Asn Ser Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly                 405 410 415 Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Ser Glu Thr Gln             420 425 430 Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser         435 440 445 Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly Phe Pro     450 455 460 Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val 465 470 475 480 Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln                 485 490 495 Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser             500 505 510 Lys Val Ile Lys Gly Ser Leu Pro Leu Ile Gly Glu Ala Asp Thr Lys         515 520 525 Thr Glu Val Gln Glu Leu Lys Asp Thr Pro Ala Val Val Ser Ala Asp     530 535 540 Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr Asp Ala Asn 545 550 555 560 Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn Gly Lys Thr                 565 570 575 Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr Tyr Ala Ala             580 585 590 Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr Thr Ser Tyr         595 600 605 Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln Leu Gly Gly     610 615 620 Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys Thr Tyr Asn 625 630 635 640 Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro Glu Leu Ala                 645 650 655 Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys Ile Asp Ala             660 665 670 Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly Ala Val Gln         675 680 685 Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr Val Asn Asn     690 695 700 Leu Ser Glu Ala Arg Ser Ile Glu Asp Ser Asp Tyr Ala Thr Glu 705 710 715 720 Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala Gly Thr Ser                 725 730 735 Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu Ser Leu Leu             740 745 750 Arg      <210> 263 <211> 584 <212> PRT <213> Artificial Sequence <220> <223> Influenza B / Wisonsin / 1/2010 HA <400> 263 Met Lys Ala Ile Ile Val Leu Leu Met Val Val Thr Ser Asn Ala Asp  1 5 10 15 Arg Ile Cys Thr Gly Ile Thr Ser Ser Asn Ser Pro His Val Val Lys             20 25 30 Thr Ala Thr Gln Gly Glu Val Asn Val Thr Gly Val Ile Pro Leu Thr         35 40 45 Thr Thr Pro Thr Lys Ser Tyr Phe Ala Asn Leu Lys Gly Thr Arg Thr     50 55 60 Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val 65 70 75 80 Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala                 85 90 95 Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile             100 105 110 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly         115 120 125 Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys     130 135 140 Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn 145 150 155 160 Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro                 165 170 175 Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro             180 185 190 Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His         195 200 205 Ser Asp Asn Lys Thr Gln Met Lys Ser Leu Tyr Gly Asp Ser Asn Pro     210 215 220 Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser 225 230 235 240 Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln                 245 250 255 Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr             260 265 270 Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp         275 280 285 Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile     290 295 300 Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys Ser 305 310 315 320 Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys Pro                 325 330 335 Ile Trp Val Lys Thr Pro Leu Lys Leu Ala Asn Gly Thr Lys Tyr Arg             340 345 350 Pro Pro Ala Lys Leu Leu Lys Glu Arg Gly Phe Phe Gly Ala Ile Ala         355 360 365 Gly Phe Leu Glu Gly Gly Trp Glu Gly Met Ile Ala Gly Trp His Gly     370 375 380 Tyr Thr Ser His Gly Ala His Gly Val Ala Val Ala Ala Asp Leu Lys 385 390 395 400 Ser Thr Gln Glu Ala Ile Asn Lys Ile Thr Lys Asn Leu Asn Ser Leu                 405 410 415 Ser Glu Leu Glu Val Lys Asn Leu Gln Arg Leu Ser Gly Ala Met Asp             420 425 430 Glu Leu His Asn Glu Ile Leu Glu Leu Asp Glu Lys Val Asp Asp Leu         435 440 445 Arg Ala Asp Thr Ile Ser Ser Gln Ile Glu Leu Ala Val Leu Leu Ser     450 455 460 Asn Glu Gly Ile Asle Ser Glu Asp Glu His Leu Leu Ala Leu Glu 465 470 475 480 Arg Lys Leu Lys Lys Met Leu Gly Pro Ser Ala Val Asp Ile Gly Asn                 485 490 495 Gly Cys Phe Glu Thr Lys His Lys Cys Asn Gln Thr Cys Leu Asp Arg             500 505 510 Ile Ala Gly Thr Phe Asn Ala Gly Glu Phe Ser Leu Pro Thr Phe         515 520 525 Asp Ser Leu Asn Ile Thr Ala Ala Ser Leu Asn Asp Asp Gly Leu Asp     530 535 540 Asn His Thr Ile Leu Leu Tyr Tyr Ser Thr Ala Ala Ser Ser Leu Ala 545 550 555 560 Val Thr Leu Met Leu Ala Ile Phe Ile Val Tyr Met Val Ser Ser Asp                 565 570 575 Asn Val Ser Cys Ser Ile Cys Leu             580 <210> 264 <211> 585 <212> PRT <213> Artificial Sequence <220> <223> Influenza B / Brisbane / 60/2008 HA <400> 264 Met Lys Ala Ile Ile Val Leu Leu Met Val Val Thr Ser Asn Ala Asp  1 5 10 15 Arg Ile Cys Thr Gly Ile Thr Ser Ser Asn Ser Pro His Val Val Lys             20 25 30 Thr Ala Thr Gln Gly Glu Val Asn Val Thr Gly Val Ile Pro Leu Thr         35 40 45 Thr Thr Pro Thr Lys Ser His Phe Ala Asn Leu Lys Gly Thr Glu Thr     50 55 60 Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp Val 65 70 75 80 Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg Val                 85 90 95 Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile             100 105 110 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly         115 120 125 Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn Ala Glu Asn     130 135 140 Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro Asn 145 150 155 160 Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro                 165 170 175 Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu Val             180 185 190 Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe         195 200 205 His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser Lys     210 215 220 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val 225 230 235 240 Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu Pro                 245 250 255 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly Lys             260 265 270 Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys Val         275 280 285 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu     290 295 300 Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys 305 310 315 320 Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys                 325 330 335 Pro Ile Trp Val Lys Thr Pro Leu Lys Leu Ala Asn Gly Thr Lys Tyr             340 345 350 Arg Pro Pro Ala Lys Leu Leu Lys Glu Arg Gly Phe Phe Gly Ala Ile         355 360 365 Ala Gly Phe Leu Glu Gly Gly Trp Glu Gly Met Ile Ala Gly Trp His     370 375 380 Gly Tyr Thr Ser His Gly Ala His Gly Val Ala Val Ala Ala Asp Leu 385 390 395 400 Lys Ser Thr Gln Glu Ala Ile Asn Lys Ile Thr Lys Asn Leu Asn Ser                 405 410 415 Leu Ser Glu Leu Glu Val Lys Asn Leu Gln Arg Leu Ser Gly Ala Met             420 425 430 Asp Glu Leu His Asn Glu Ile Leu Glu Leu Asp Glu Lys Val Asp Asp         435 440 445 Leu Arg Ala Asp Thr Ile Ser Ser Gln Ile Glu Leu Ala Val Leu Leu     450 455 460 Ser Asn Glu Gly Ile Asle Ser Glu Asp Glu His Leu Leu Ala Leu 465 470 475 480 Glu Arg Lys Leu Lys Lys Met Leu Gly Pro Ser Ala Val Glu Ile Gly                 485 490 495 Asn Gly Cys Phe Glu Thr Lys His Lys Cys Asn Gln Thr Cys Leu Asp             500 505 510 Arg Ile Ala Ala Gly Thr Phe Asp Ala Gly Glu Phe Ser Leu Pro Thr         515 520 525 Phe Asp Ser Leu Asn Ile Thr Ala Ala Ser Leu Asn Asp Asp Gly Leu     530 535 540 Asp Asn His Thr Ile Leu Leu Tyr Tyr Ser Thr Ala Ala Ser Seru 545 550 555 560 Ala Val Thr Leu Met Ile Ala Ile Phe Val Val Tyr Met Val Ser Arg                 565 570 575 Asp Asn Val Ser Cys Ser Ile Cys Leu             580 585 <210> 265 <211> 585 <212> PRT <213> Artificial Sequence <220> <223> Influenza B / Bangladesh / 5495/2009 HA <400> 265 Met Lys Ala Ile Ile Val Leu Leu Met Val Val Thr Ser Asn Ala Asp  1 5 10 15 Arg Ile Cys Thr Gly Ile Thr Ser Ser Asn Ser Pro His Val Val Lys             20 25 30 Thr Ala Thr Gln Gly Glu Val Asn Val Thr Gly Val Ile Pro Leu Thr         35 40 45 Thr Thr Pro Thr Lys Ser His Phe Ala Asn Leu Lys Gly Thr Glu Thr     50 55 60 Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp Val 65 70 75 80 Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg Val                 85 90 95 Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile             100 105 110 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly         115 120 125 Tyr Glu His Ile Arg Leu Ser Thr Asn Asn Val Ile Asn Ala Glu Asn     130 135 140 Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro Asn 145 150 155 160 Val Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro                 165 170 175 Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu Val             180 185 190 Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe         195 200 205 His Ser Asp Asn Glu Ile Gln Met Ala Lys Leu Tyr Gly Asp Ser Arg     210 215 220 Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val 225 230 235 240 Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu Pro                 245 250 255 Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys Ser Gly Lys             260 265 270 Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys Val         275 280 285 Trp Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu     290 295 300 Ile Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys 305 310 315 320 Ser Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys                 325 330 335 Pro Ile Trp Val Lys Thr Pro Leu Lys Leu Ala Asn Gly Thr Lys Tyr             340 345 350 Arg Pro Pro Ala Lys Leu Leu Lys Glu Arg Gly Phe Phe Gly Ala Ile         355 360 365 Ala Gly Phe Leu Glu Gly Gly Trp Glu Gly Met Ile Ala Gly Trp His     370 375 380 Gly Tyr Thr Ser His Gly Ala His Gly Val Ala Val Ala Ala Asp Leu 385 390 395 400 Lys Ser Thr Gln Glu Ala Ile Asn Lys Ile Thr Lys Asn Leu Asn Ser                 405 410 415 Leu Ser Glu Leu Glu Val Lys Asn Leu Gln Arg Leu Ser Gly Ala Met             420 425 430 Asp Glu Leu His Asn Glu Ile Leu Glu Leu Asp Glu Lys Val Asp Asp         435 440 445 Leu Arg Ala Asp Thr Ile Ser Ser Gln Ile Glu Leu Ala Val Leu Leu     450 455 460 Ser Asn Glu Gly Ile Asle Ser Glu Asp Glu His Leu Leu Ala Leu 465 470 475 480 Glu Arg Lys Leu Lys Lys Met Leu Gly Pro Ser Ala Val Glu Ile Gly                 485 490 495 Asn Gly Cys Phe Glu Thr Lys His Lys Cys Asn Gln Thr Cys Leu Asp             500 505 510 Arg Ile Ala Ala Gly Thr Phe Asp Ala Gly Glu Phe Ser Leu Pro Thr         515 520 525 Phe Asp Ser Leu Asn Ile Thr Ala Ala Ser Leu Asn Asp Asp Gly Leu     530 535 540 Asp Asn His Thr Ile Leu Leu Tyr Tyr Ser Thr Ala Ala Ser Seru 545 550 555 560 Ala Val Thr Leu Met Ile Ala Ile Phe Val Val Tyr Met Val Ser Arg                 565 570 575 Asp Asn Val Ser Cys Ser Ile Cys Leu             580 585 <210> 266 <211> 584 <212> PRT <213> Artificial Sequence <220> <223> Influenza B / Hubei-Wujiagang / 158/2009 HA <400> 266 Met Lys Ala Ile Ile Val Leu Leu Met Val Val Thr Ser Asn Ala Asp  1 5 10 15 Arg Ile Cys Thr Gly Ile Thr Ser Ser Asn Ser Pro His Val Val Lys             20 25 30 Thr Ala Thr Gln Gly Glu Val Asn Val Thr Gly Val Ile Pro Leu Thr         35 40 45 Thr Thr Pro Thr Lys Ser Tyr Phe Ala Asn Leu Lys Gly Thr Arg Thr     50 55 60 Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val 65 70 75 80 Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala                 85 90 95 Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile             100 105 110 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly         115 120 125 Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys     130 135 140 Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn 145 150 155 160 Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro                 165 170 175 Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro             180 185 190 Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His         195 200 205 Ser Asp Asn Lys Asn Gln Met Lys Ser Leu Tyr Gly Asp Ser Asn Pro     210 215 220 Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser 225 230 235 240 Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln                 245 250 255 Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr             260 265 270 Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp         275 280 285 Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile     290 295 300 Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys Ser 305 310 315 320 Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys Pro                 325 330 335 Ile Trp Val Lys Thr Pro Leu Lys Leu Ala Asn Gly Thr Lys Tyr Arg             340 345 350 Pro Pro Ala Lys Leu Leu Lys Glu Arg Gly Phe Phe Gly Ala Ile Ala         355 360 365 Gly Phe Leu Glu Gly Gly Trp Glu Gly Met Ile Ala Gly Trp His Gly     370 375 380 Tyr Thr Ser His Gly Ala His Gly Val Ala Val Ala Ala Asp Leu Lys 385 390 395 400 Ser Thr Gln Glu Ala Ile Asn Lys Ile Thr Lys Asn Leu Asn Ser Leu                 405 410 415 Ser Glu Leu Glu Val Lys Asn Leu Gln Arg Leu Ser Gly Ala Met Asp             420 425 430 Glu Leu His Asn Glu Ile Leu Glu Leu Asp Glu Lys Val Asp Asp Leu         435 440 445 Arg Ala Asp Thr Ile Ser Ser Gln Ile Glu Leu Ala Val Leu Leu Ser     450 455 460 Asn Glu Gly Ile Asle Ser Glu Asp Glu His Leu Leu Ala Leu Glu 465 470 475 480 Arg Lys Leu Lys Lys Met Leu Gly Pro Ser Ala Val Asp Ile Gly Asn                 485 490 495 Gly Cys Phe Glu Thr Lys His Lys Cys Asn Gln Thr Cys Leu Asp Arg             500 505 510 Ile Ala Gly Thr Phe Asn Ala Gly Glu Phe Ser Leu Pro Thr Phe         515 520 525 Asp Ser Leu Asn Ile Thr Ala Ala Ser Leu Asn Asp Asp Gly Leu Asp     530 535 540 Asn His Thr Ile Leu Leu Tyr Tyr Ser Thr Ala Ala Ser Ser Leu Ala 545 550 555 560 Val Thr Leu Met Leu Ala Ile Phe Ile Val Tyr Met Val Ser Ser Asp                 565 570 575 Asn Val Ser Cys Ser Ile Cys Leu             580 <210> 267 <211> 584 <212> PRT <213> Artificial Sequence <220> <223> Influenza B / Texas / 6/2011 HA <400> 267 Met Lys Ala Ile Ile Val Leu Leu Met Val Val Thr Ser Asn Ala Asp  1 5 10 15 Arg Ile Cys Thr Gly Ile Thr Ser Ser Asn Ser Pro His Val Val Lys             20 25 30 Thr Ala Thr Gln Gly Glu Val Asn Val Thr Gly Val Ile Pro Leu Thr         35 40 45 Thr Thr Pro Thr Lys Ser Tyr Phe Ala Asn Leu Lys Gly Thr Arg Thr     50 55 60 Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu Asp Val 65 70 75 80 Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala Lys Ala                 85 90 95 Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile             100 105 110 Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly         115 120 125 Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala Glu Lys     130 135 140 Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys Pro Asn 145 150 155 160 Ala Thr Ser Lys Ile Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro                 165 170 175 Lys Asp Asn Tyr Lys Asn Ala Thr Asn Pro Leu Thr Val Glu Val Pro             180 185 190 Tyr Ile Cys Lys Glu Glu Glu Asp Gln Ile Thr Val Trp Gly Phe His         195 200 205 Ser Asp Asn Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser Asn Pro     210 215 220 Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser 225 230 235 240 Gln Ile Gly Asp Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu Pro Gln                 245 250 255 Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly Lys Thr             260 265 270 Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys Val Trp         275 280 285 Cys Ala Ser Gly Arg Ser Lys Val Ile Lys Gly Ser Leu Pro Leu Ile     290 295 300 Gly Glu Ala Asp Cys Leu His Glu Lys Tyr Gly Gly Leu Asn Lys Ser 305 310 315 320 Lys Pro Tyr Tyr Thr Gly Gly His Ala Lys Ala Ile Gly Asn Cys Pro                 325 330 335 Ile Trp Val Lys Thr Pro Leu Lys Leu Ala Asn Gly Thr Lys Tyr Arg             340 345 350 Pro Pro Ala Lys Leu Leu Lys Glu Arg Gly Phe Phe Gly Ala Ile Ala         355 360 365 Gly Phe Leu Glu Gly Gly Trp Glu Gly Met Ile Ala Gly Trp His Gly     370 375 380 Tyr Thr Ser His Gly Ala His Gly Val Ala Val Ala Ala Asp Leu Lys 385 390 395 400 Ser Thr Gln Glu Ala Ile Asn Lys Ile Thr Lys Asn Leu Asn Ser Leu                 405 410 415 Ser Glu Leu Glu Val Lys Asn Leu Gln Arg Leu Ser Gly Ala Met Asp             420 425 430 Glu Leu His Asn Glu Ile Leu Glu Leu Asp Glu Lys Val Asp Asp Leu         435 440 445 Arg Ala Asp Thr Ile Ser Ser Gln Ile Glu Leu Ala Val Leu Leu Ser     450 455 460 Asn Glu Gly Ile Asle Ser Glu Asp Glu His Leu Leu Ala Leu Glu 465 470 475 480 Arg Lys Leu Lys Lys Met Leu Gly Pro Ser Ala Val Asp Ile Gly Asn                 485 490 495 Gly Cys Phe Glu Thr Lys His Lys Cys Asn Gln Thr Cys Leu Asp Arg             500 505 510 Ile Ala Gly Thr Phe Asn Ala Gly Glu Phe Ser Leu Pro Thr Phe         515 520 525 Asp Ser Leu Asn Ile Thr Ala Ala Ser Leu Asn Asp Asp Gly Leu Asp     530 535 540 Asn His Thr Ile Leu Leu Tyr Tyr Ser Thr Ala Ala Ser Ser Leu Ala 545 550 555 560 Val Thr Leu Met Leu Ala Ile Phe Ile Val Tyr Met Val Ser Ser Asp                 565 570 575 Asn Val Ser Cys Ser Ile Cys Leu             580 <210> 268 <211> 852 <212> PRT <213> Artificial Sequence <220> <223> HL186 STF2.R3.2x.HA1-2 CA07 <400> 268 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Gly Val             180 185 190 Ala Pro Leu His Leu Gly Lys Cys Asn Ile Ala Gly Trp Ile Leu Gly         195 200 205 Asn Pro Glu Cys Glu Ser Leu Ser Thr Ala Ser Ser Trp Ser Tyr Ile     210 215 220 Val Glu Thr Pro Ser Ser Asp Asn Gly Thr Cys Tyr Pro Gly Asp Phe 225 230 235 240 Ile Asp Tyr Glu Glu Leu Arg Glu Gln Leu Ser Ser Val Ser Ser Phe                 245 250 255 Glu Arg Phe Glu Ile Phe Pro Lys Thr Ser Ser Trp Pro Asn His Asp             260 265 270 Ser Asn Lys Gly Val Thr Ala Ala Cys Pro His Ala Gly Ala Lys Ser         275 280 285 Phe Tyr Lys Asn Leu Ile Trp Leu Val Lys Lys Gly Asn Ser Tyr Pro     290 295 300 Lys Leu Ser Lys Ser Tyr Ile Asn Asp Lys Gly Lys Glu Val Leu Val 305 310 315 320 Leu Trp Gly Ile His His Pro Ser Thr Ser Ala Asp Gln Gln Ser Leu                 325 330 335 Tyr Gln Asn Ala Asp Ala Tyr Val Phe Val Gly Ser Ser Arg Tyr Ser             340 345 350 Lys Lys Phe Lys Pro Glu Ile Ala Ile Arg Pro Lys Val Arg Asp Gln         355 360 365 Glu Gly Arg Met Met Asn Tyr Tyr Trp Thr Leu Val Glu Pro Gly Asp Lys     370 375 380 Ile Thr Phe Glu Ala Thr Gly Asn Leu Val Val Pro Arg Tyr Ala Phe 385 390 395 400 Ala Met Glu Arg Asn Ala Gly Ser Gly Ile Ile Ser Ser Val Val                 405 410 415 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr             420 425 430 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn         435 440 445 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr     450 455 460 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr 465 470 475 480 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln                 485 490 495 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys             500 505 510 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro         515 520 525 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys     530 535 540 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly 545 550 555 560 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr                 565 570 575 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr             580 585 590 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala         595 600 605 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu     610 615 620 Ser Leu Leu Ala Ser Gly Val Ala Pro Leu His Leu Gly Lys Cys Asn 625 630 635 640 Ile Ala Gly Trp Ile Leu Gly Asn Pro Glu Cys Glu Ser Leu Ser Thr                 645 650 655 Ala Ser Ser Trp Ser Tyr Ile Val Glu Thr Ser Ser Asp Asn Gly             660 665 670 Thr Cys Tyr Pro Gly Asp Phe Ile Asp Tyr Glu Glu Leu Arg Glu Gln         675 680 685 Leu Ser Ser Val Ser Ser Phe Glu Arg Phe Glu Ile Phe Pro Lys Thr     690 695 700 Ser Ser Trp Pro Asn His Asp Ser Asn Lys Gly Val Thr Ala Ala Cys 705 710 715 720 Pro His Ala Gly Ala Lys Ser Phe Tyr Lys Asn Leu Ile Trp Leu Val                 725 730 735 Lys Lys Gly Asn Ser Tyr Pro Lys Leu Ser Lys Ser Tyr Ile Asn Asp             740 745 750 Lys Gly Lys Glu Val Leu Val Leu Trp Gly Ile His His Pro Ser Thr         755 760 765 Ser Ala Asp Gln Gln Ser Leu Tyr Gln Asn Ala Asp Ala Tyr Val Phe     770 775 780 Val Gly Ser Ser Arg Tyr Ser Lys Lys Phe Lys Pro Glu Ile Ala Ile 785 790 795 800 Arg Pro Lys Val Arg Asp Gln Glu Gly Arg Met Asn Tyr Tyr Trp Thr                 805 810 815 Leu Val Glu Pro Gly Asp Lys Ile Thr Phe Glu Ala Thr Gly Asn Leu             820 825 830 Val Val Pro Arg Tyr Ala Phe Ala Met Glu Arg Asn Ala Gly Ser Gly         835 840 845 Ile Ile Ile Ser     850 <210> 269 <211> 680 <212> PRT <213> Artificial Sequence <220> <223> HL490 STF2.R3.HA1-1L PE16 <400> 269 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Glu Leu             180 185 190 Val Gln Ser Ser Ser Thr Gly Glu Ile Cys Asp Ser Pro His Gln Ile         195 200 205 Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly Asp Pro     210 215 220 Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Tyr Val Glu Arg 225 230 235 240 Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Serp                 245 250 255 Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe Asn Asn             260 265 270 Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser Ser Ala         275 280 285 Cys Ile Arg Arg Ser Lys Asn Ser Phe Phe Ser Arg Leu Asn Trp Leu     290 295 300 Thr His Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr Met Pro Asn 305 310 315 320 Asn Glu Gln Phe Asp Lys Leu Tyr Val Trp Gly Val His His Pro Gly                 325 330 335 Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ala Ser Gly Arg Ile             340 345 350 Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ser Pro Asn Ile Gly         355 360 365 Ser Arg Pro Arg Val Arg Asn Ile Pro Ser Arg Ile Ser Ile Tyr Trp     370 375 380 Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr Gly Asn 385 390 395 400 Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys Ser Ser                 405 410 415 Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu Cys Ile             420 425 430 Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn Val Asn         435 440 445 Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asp Thr Leu     450 455 460 Glu Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly 465 470 475 480 Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr                 485 490 495 Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala             500 505 510 Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile         515 520 525 Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr     530 535 540 Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr 545 550 555 560 Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe                 565 570 575 Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn             580 585 590 Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg         595 600 605 Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn     610 615 620 Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu 625 630 635 640 Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile                 645 650 655 Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro             660 665 670 Gln Asn Val Leu Ser Leu Leu Arg         675 680 <210> 270 <211> 506 <212> PRT <213> Artificial Sequence <220> <223> Flagellin (FljB) with GG mutations <400> 270 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Gly Gly Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Gly Ala Thr Thr Lys Thr Glu Val Gln Glu Leu Lys         275 280 285 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala     290 295 300 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met 305 310 315 320 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu                 325 330 335 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly             340 345 350 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr         355 360 365 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val     370 375 380 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His 385 390 395 400 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr                 405 410 415 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala             420 425 430 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile         435 440 445 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg     450 455 460 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala 465 470 475 480 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln                 485 490 495 Val Pro Gln Asn Val Leu Ser Leu Leu Ala             500 505 <210> 271 <211> 404 <212> PRT <213> Artificial Sequence <220> <223> Flagellin (FljB) D3 removed <400> 271 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Gly Lys Ala Ala Val Val             180 185 190 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr         195 200 205 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn     210 215 220 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr 225 230 235 240 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr                 245 250 255 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln             260 265 270 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys         275 280 285 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro     290 295 300 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys 305 310 315 320 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly                 325 330 335 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr             340 345 350 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr         355 360 365 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala     370 375 380 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu 385 390 395 400 Ser Leu Leu Arg                  <210> 272 <211> 404 <212> PRT <213> Artificial Sequence <220> <223> Flagellin (FljB) D3 removed with R to A mutation <400> 272 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Gly Lys Ala Ala Val Val             180 185 190 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr         195 200 205 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn     210 215 220 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr 225 230 235 240 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr                 245 250 255 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln             260 265 270 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys         275 280 285 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro     290 295 300 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys 305 310 315 320 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly                 325 330 335 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr             340 345 350 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr         355 360 365 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala     370 375 380 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu 385 390 395 400 Ser Leu Leu Ala                  <210> 273 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Wyoming / 03/2003 HA1-1L modified <400> 273 Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Tyr Val         35 40 45 Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asn Glu Ser Phe Asn Trp Ala Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ala Cys Lys Arg Arg Ser Asn Lys Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr His Leu Lys Tyr Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Val Trp Gly Val His His     130 135 140 Pro Val Thr Asp Ser Asp Gln Ile Ser Leu Tyr Ala Gln Ala Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn                 165 170 175 Ile Gly Tyr Arg Pro Arg Val Arg Asp Ile Ser Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asp             260 265 270 Thr Leu Glu         275 <210> 274 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / New York / 2782/2004 HA1-1L modified <400> 274 Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Tyr Val         35 40 45 Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ser Cys Lys Arg Arg Ser Asn Asn Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Val Trp Gly Val His His     130 135 140 Pro Val Thr Asp Asn Asp Gln Ile Arg Leu Tyr Ala Gln Ala Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn                 165 170 175 Ile Gly Ser Arg Pro Arg Val Arg Asp Ile Pro Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asp             260 265 270 Thr Leu Glu         275 <210> 275 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Victoria / 361/2011 HA1-1L modified <400> 275 Glu Leu Val Gln Asn Ser Ser Thr Gly Glu Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Tyr Val         35 40 45 Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ala Cys Ile Arg Arg Ser Lys Asn Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr Asn Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Val Trp Gly Val His His     130 135 140 Pro Val Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ala Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn                 165 170 175 Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Met Gln Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asp             260 265 270 Thr Leu Glu         275 <210> 276 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Aichi / 2/68 HA1-1L modified <400> 276 Glu Leu Val Gln Ser Ser Ser Thr Gly Lys Ile Cys Asn Asn Pro His  1 5 10 15 Arg Ile Leu Asp Gly Ile Asp Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro His Cys Asp Val Phe Gln Asn Glu Thr Trp Asp Leu Tyr Val         35 40 45 Glu Arg Ser Ser Ala Phe Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Ile Thr Glu Gly Phe Thr Trp Thr Gly Val Thr Gln Asn Gly Gly Ser                 85 90 95 Asn Cys Lys Arg Gly Pro Gly Ser Gly Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr Lys Ser Gly Ser Thr Tyr Pro Val Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Asp Asn Phe Asp Lys Leu Tyr Val Trp Gly Val His His     130 135 140 Pro Ser Thr Asn Gln Glu Gln Thr Ser Leu Tyr Val Gln Ala Ser Gly 145 150 155 160 Arg Val Thr Val Ser Thr Arg Arg Ser Gln Gln Thr Ile Ile Pro Asn                 165 170 175 Ile Gly Ser Arg Pro Trp Val Arg Gly Leu Ser Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Val Leu Val Ile Asn Ser Asn         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Met Arg Thr Gly Lys     210 215 220 Ser Ser Ile Met Ser Ser Asp Ala Pro Ile Asp Thr Cys Ile Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Lys Ile Thr Tyr Gly Ala Cys Pro Lys Tyr Val Lys Gln Asp             260 265 270 Thr Leu Glu         275 <210> 277 <211> 275 <212> PRT <213> Artificial Sequence <220> <223> A / Wisconsin / 67/2005 HA1-1L modified <400> 277 Glu Leu Val Gln Ser Ser Ser Thr Gly Glu Ile Cys Asp Ser Pro His  1 5 10 15 Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp Ala Leu Leu Gly             20 25 30 Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp Asp Leu Tyr Val         35 40 45 Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr Asp Val Pro Asp     50 55 60 Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly Thr Leu Glu Phe 65 70 75 80 Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln Asn Gly Thr Ser                 85 90 95 Ser Ala Cys Ile Arg Arg Ser Lys Asn Ser Phe Phe Ser Arg Leu Asn             100 105 110 Trp Leu Thr His Leu Asn Phe Lys Tyr Pro Ala Leu Asn Val Thr Met         115 120 125 Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Val Trp Gly Val His His     130 135 140 Pro Gly Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala Gln Ala Ser Gly 145 150 155 160 Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr Val Ile Pro Asn                 165 170 175 Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser Arg Ile Ser Ile             180 185 190 Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu Ile Asn Ser Thr         195 200 205 Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile Arg Ser Gly Lys     210 215 220 Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys Cys Asn Ser Glu 225 230 235 240 Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys Pro Phe Gln Asn                 245 250 255 Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr Val Lys Gln Asp             260 265 270 Thr Leu Glu         275 <210> 278 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L WY03 D31-o1 with mutations <400> 278 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys         275 280 285 Asp Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp 305 310 315 320 Asp Leu Tyr Val Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Ala Gly Val Thr Gln         355 360 365 Asn Gly Thr Ser Ser Ala Cys Lys Arg Arg Ser Asn Lys Ser Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr His Leu Lys Tyr Lys Tyr Pro Ala Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Val Trp                 405 410 415 Gly Val His His Pro Val Thr Asp Ser Asp Gln Ile Ser Leu Tyr Ala             420 425 430 Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr         435 440 445 Val Ile Pro Asn Ile Gly Tyr Arg Pro Arg Val Arg Asp Ile Ser Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu 465 470 475 480 Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile                 485 490 495 Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys             500 505 510 Cys Asn Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr     530 535 540 Val Lys Gln Asp Thr Leu Glu Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 279 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L NY2782 D3I-o1 with mutations <400> 279 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Gly Ile Cys         275 280 285 Asp Ser Pro His Gln Ile Leu Asp Gly Glu Asn Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp 305 310 315 320 Asp Leu Tyr Val Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln         355 360 365 Asn Gly Thr Ser Ser Ser Cys Lys Arg Arg Ser Asn Ser Ser Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr His Leu Lys Phe Lys Tyr Pro Ala Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Glu Lys Phe Asp Lys Leu Tyr Val Trp                 405 410 415 Gly Val His His Pro Val Thr Asp Asn Asp Gln Ile Arg Leu Tyr Ala             420 425 430 Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr         435 440 445 Val Ile Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asp Ile Pro Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu 465 470 475 480 Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile                 485 490 495 Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys             500 505 510 Cys Asn Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr     530 535 540 Val Lys Gln Asp Thr Leu Glu Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 280 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L VT361 D3I-o1 with mutations <400> 280 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Asn Ser Ser Thr Gly Glu Ile Cys         275 280 285 Asp Ser Pro His Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp 305 310 315 320 Asp Leu Tyr Val Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln         355 360 365 Asn Gly Thr Ser Ser Ala Cys Ile Arg Ser Ser Lys Asn Ser Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr Asn Leu Asn Phe Lys Tyr Pro Ala Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Val Trp                 405 410 415 Gly Val His His Pro Val Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala             420 425 430 Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr         435 440 445 Val Ile Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu 465 470 475 480 Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Met                 485 490 495 Gln Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys             500 505 510 Cys Asn Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr     530 535 540 Val Lys Gln Asp Thr Leu Glu Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 281 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L Aichi2 D3I-o1 with mutations <400> 281 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Lys Ile Cys         275 280 285 Asn Asn Pro His Arg Ile Leu Asp Gly Ile Asp Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro His Cys Asp Val Phe Gln Asn Glu Thr Trp 305 310 315 320 Asp Leu Tyr Val Glu Arg Ser Ser Ala Phe Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Ile Thr Glu Gly Phe Thr Trp Thr Gly Val Thr Gln         355 360 365 Asn Gly Gly Ser Asn Ala Cys Lys Arg Gly Pro Gly Ser Gly Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr Lys Ser Gly Ser Thr Tyr Pro Val Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Asp Asn Phe Asp Lys Leu Tyr Val Trp                 405 410 415 Gly Val His His Pro Ser Thr Asn Gln Glu Gln Thr Ser Leu Tyr Val             420 425 430 Gln Ala Ser Gly Arg Val Thr Val Ser Thr Arg Arg Ser Gln Gln Thr         435 440 445 Ile Ile Pro Asn Ile Gly Ser Arg Pro Trp Val Arg Gly Leu Ser Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Val Leu Val 465 470 475 480 Ile Asn Ser Asn Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Met                 485 490 495 Arg Thr Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Asp Thr             500 505 510 Cys Ile Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Lys Ile Thr Tyr Gly Ala Cys Pro Lys Tyr     530 535 540 Val Lys Gln Asp Thr Leu Glu Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 282 <211> 778 <212> PRT <213> Artificial Sequence <220> <223> STF2.D3Ins.HA1-1L WI67 D3I-o1 with mutations <400> 282 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Tyr Ala             180 185 190 Asn Asn Gly Thr Thr Leu Asp Val Ser Gly Leu Asp Asp Ala Ala Ile         195 200 205 Lys Ala Ala Thr Gly Gly Thr Asn Gly Thr Ala Ser Val Thr Gly Gly     210 215 220 Ala Val Lys Phe Asp Ala Asp Asn Asn Lys Tyr Phe Val Thr Ile Gly 225 230 235 240 Gly Phe Thr Gly Ala Asp Ala Ala Lys Asn Gly Asp Tyr Glu Val Asn                 245 250 255 Val Ala Thr Asp Gly Thr Val Thr Leu Ala Ala Gly Ala Thr Lys Thr             260 265 270 Thr Met Pro Ala Glu Leu Val Gln Ser Ser Ser Thr Gly Glu Ile Cys         275 280 285 Asp Ser Pro His Gln Ile Leu Asp Gly Lys Asn Cys Thr Leu Ile Asp     290 295 300 Ala Leu Leu Gly Asp Pro Gln Cys Asp Gly Phe Gln Asn Lys Lys Trp 305 310 315 320 Asp Leu Tyr Val Glu Arg Ser Ser Ala Tyr Ser Asn Cys Tyr Pro Tyr                 325 330 335 Asp Val Pro Asp Tyr Ala Ser Leu Arg Ser Leu Val Ala Ser Ser Gly             340 345 350 Thr Leu Glu Phe Asn Asn Glu Ser Phe Asn Trp Thr Gly Val Thr Gln         355 360 365 Asn Gly Thr Ser Ser Ala Cys Ile Arg Ser Ser Lys Asn Ser Phe Phe     370 375 380 Ser Arg Leu Asn Trp Leu Thr His Leu Asn Phe Lys Tyr Pro Ala Leu 385 390 395 400 Asn Val Thr Met Pro Asn Asn Glu Gln Phe Asp Lys Leu Tyr Val Trp                 405 410 415 Gly Val His His Pro Gly Thr Asp Lys Asp Gln Ile Phe Leu Tyr Ala             420 425 430 Gln Ala Ser Gly Arg Ile Thr Val Ser Thr Lys Arg Ser Gln Gln Thr         435 440 445 Val Ile Pro Asn Ile Gly Ser Arg Pro Arg Val Arg Asn Ile Pro Ser     450 455 460 Arg Ile Ser Ile Tyr Trp Thr Ile Val Lys Pro Gly Asp Ile Leu Leu 465 470 475 480 Ile Asn Ser Thr Gly Asn Leu Ile Ala Pro Arg Gly Tyr Phe Lys Ile                 485 490 495 Arg Ser Gly Lys Ser Ser Ile Met Arg Ser Asp Ala Pro Ile Gly Lys             500 505 510 Cys Asn Ser Glu Cys Ile Thr Pro Asn Gly Ser Ile Pro Asn Asp Lys         515 520 525 Pro Phe Gln Asn Val Asn Arg Ile Thr Tyr Gly Ala Cys Pro Arg Tyr     530 535 540 Val Lys Gln Asp Thr Leu Glu Thr Lys Thr Glu Val Gln Glu Leu Lys 545 550 555 560 Asp Thr Pro Ala Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala                 565 570 575 Gly Gly Val Asp Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met             580 585 590 Ser Tyr Thr Asp Lys Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu         595 600 605 Lys Ala Gly Asp Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly     610 615 620 Ala Ile Lys Ala Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr 625 630 635 640 Lys Thr Ala Ala Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val                 645 650 655 Val Thr Ile Asp Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His             660 665 670 Asp Phe Lys Ala Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr         675 680 685 Glu Asn Pro Leu Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala     690 695 700 Leu Arg Ser Asp Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile 705 710 715 720 Thr Asn Leu Gly Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Arg                 725 730 735 Ile Glu Asp Ser Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Ser Ala             740 745 750 Gln Ile Leu Gln Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln         755 760 765 Val Pro Gln Asn Val Leu Ser Leu Leu Arg     770 775 <210> 283 <211> 405 <212> PRT <213> Artificial Sequence <220> <223> Flagellin (FljB) D3 removed native <400> 283 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Ala Val             180 185 190 Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala         195 200 205 Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys     210 215 220 Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys 225 230 235 240 Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys                 245 250 255 Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn             260 265 270 Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly         275 280 285 Lys Thr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln     290 295 300 Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln 305 310 315 320 Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu                 325 330 335 Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn             340 345 350 Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp         355 360 365 Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln     370 375 380 Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val 385 390 395 400 Leu Ser Leu Leu Arg                 405 <210> 284 <211> 405 <212> PRT <213> Artificial Sequence <220> <223> Flagellin (FljB) D3 removed with R to A mutation <400> 284 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Ala Val             180 185 190 Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala         195 200 205 Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys     210 215 220 Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys 225 230 235 240 Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys                 245 250 255 Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn             260 265 270 Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly         275 280 285 Lys Thr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln     290 295 300 Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln 305 310 315 320 Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu                 325 330 335 Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn             340 345 350 Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp         355 360 365 Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln     370 375 380 Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val 385 390 395 400 Leu Ser Leu Leu Ala                 405 <210> 285 <211> 406 <212> PRT <213> Artificial Sequence <220> <223> Flagellin (FljB) D3 removed mutated for some R3.2x <400> 285 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Ser Val             180 185 190 Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala         195 200 205 Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys     210 215 220 Asn Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys 225 230 235 240 Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys                 245 250 255 Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn             260 265 270 Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly         275 280 285 Lys Thr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln     290 295 300 Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln 305 310 315 320 Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu                 325 330 335 Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn             340 345 350 Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp         355 360 365 Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln     370 375 380 Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val 385 390 395 400 Leu Ser Leu Leu Ala Ser                 405 <210> 286 <211> 223 <212> PRT <213> Artificial Sequence <220> <223> A / California / 07/2009, HA1-2 <400> 286 Gly Val Ala Pro Leu His Leu Gly Lys Cys Asn Ile Ala Gly Trp Ile  1 5 10 15 Leu Gly Asn Pro Glu Cys Glu Ser Leu Ser Thr Ala Ser Ser Trp Ser             20 25 30 Tyr Ile Val Glu Thr Pro Ser Ser Asp Asn Gly Thr Cys Tyr Pro Gly         35 40 45 Asp Phe Ile Asp Tyr Glu Glu Leu Arg Glu Gln Leu Ser Ser Ser Ser     50 55 60 Ser Phe Glu Arg Phe Glu Ile Phe Pro Lys Thr Ser Ser Trp Pro Asn 65 70 75 80 His Asp Ser Asn Lys Gly Val Thr Ala Ala Cys Pro His Ala Gly Ala                 85 90 95 Lys Ser Phe Tyr Lys Asn Leu Ile Trp Leu Val Lys Lys Gly Asn Ser             100 105 110 Tyr Pro Lys Leu Ser Lys Ser Tyr Ile Asn Asp Lys Gly Lys Glu Val         115 120 125 Leu Val Leu Trp Gly Ile His His Pro Ser Ser Ser Ala Asp Gln Gln     130 135 140 Ser Leu Tyr Gln Asn Ala Asp Ala Tyr Val Phe Val Gly Ser Ser Arg 145 150 155 160 Tyr Ser Lys Lys Phe Lys Pro Glu Ile Ala Ile Arg Pro Lys Val Arg                 165 170 175 Asp Gln Glu Gly Arg Met Asn Tyr Tyr Trp Thr Leu Val Glu Pro Gly             180 185 190 Asp Lys Ile Thr Phe Glu Ala Thr Gly Asn Leu Val Val Pro Arg Tyr         195 200 205 Ala Phe Ala Met Glu Arg Asn Ala Gly Ser Gly Ile Ile Ile Ser     210 215 220 <210> 287 <211> 883 <212> PRT <213> Artificial Sequence <220> <223> HL118 STF2.R3.2 HA1-2 B / FL4 <400> 287 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Ser Thr             180 185 190 Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys Leu Asn Cys Thr Asp Leu         195 200 205 Asp Val Ala Leu Gly Arg Pro Met Cys Val Gly Thr Thr Pro Ser Ala     210 215 220 Lys Ala Ser Ile Leu His Glu Val Lys Pro Val Thr Ser Gly Cys Phe 225 230 235 240 Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu Leu                 245 250 255 Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr Gln Asn Val Ile Asp Ala             260 265 270 Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu Gly Thr Ser Gly Ser Cys         275 280 285 Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe Ala Thr Met Ala Trp Ala     290 295 300 Val Pro Lys Asp Asn Asn Lys Asn Ala Thr Asn Pro Leu Thr Val Glu 305 310 315 320 Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val Trp Gly                 325 330 335 Phe His Ser Asp Asp Lys Thr Gln Met Lys Asn Leu Tyr Gly Asp Ser             340 345 350 Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr His Tyr         355 360 365 Val Ser Gln Ile Gly Ser Phe Pro Asp Gln Thr Glu Asp Gly Gly Leu     370 375 380 Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Met Gln Lys Pro Gly 385 390 395 400 Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly Val Leu Leu Pro Gln Lys                 405 410 415 Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Ser Val Val             420 425 430 Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp Ala Thr         435 440 445 Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp Lys Asn     450 455 460 Gly Lys Thr Ile Glu Gly Gly Tyr Ala Leu Lys Ala Gly Asp Lys Tyr 465 470 475 480 Tyr Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala Lys Thr                 485 490 495 Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala Asn Gln             500 505 510 Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp Gly Lys         515 520 525 Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala Gln Pro     530 535 540 Glu Leu Ala Glu Ala Ala Lys Thr Thr Glu Asn Pro Leu Gln Lys 545 550 555 560 Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp Leu Gly                 565 570 575 Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly Asn Thr             580 585 590 Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser Asp Tyr         595 600 605 Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln Gln Ala     610 615 620 Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn Val Leu 625 630 635 640 Ser Leu Leu Ala Gly Thr Arg Thr Arg Gly Lys Leu Cys Pro Asp Cys                 645 650 655 Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro Met Cys Val             660 665 670 Gly Thr Thr Pro Ser Ala Lys Ala Ser Ile Leu His Glu Val Lys Pro         675 680 685 Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg     690 695 700 Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu Asn Ile Arg Leu Ser Thr 705 710 715 720 Gln Asn Val Ile Asp Ala Glu Lys Ala Pro Gly Gly Pro Tyr Arg Leu                 725 730 735 Gly Thr Ser Gly Ser Cys Pro Asn Ala Thr Ser Lys Ser Gly Phe Phe             740 745 750 Ala Thr Met Ala Trp Ala Val Pro Lys Asp Asn Asn Lys Asn Ala Thr         755 760 765 Asn Pro Leu Thr Val Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp     770 775 780 Gln Ile Thr Val Trp Gly Phe His Ser Asp Asp Lys Thr Gln Met Lys 785 790 795 800 Asn Leu Tyr Gly Asp Ser Asn Pro Gln Lys Phe Thr Ser Ser Ala Asn                 805 810 815 Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Ser Phe Pro Asp Gln             820 825 830 Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr         835 840 845 Met Met Gln Lys Pro Gly Lys Thr Gly Thr Ile Val Tyr Gln Arg Gly     850 855 860 Val Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val 865 870 875 880 Ile Lys Gly              <210> 288 <211> 887 <212> PRT <213> Artificial Sequence <220> <223> HL171 R3.2 HA1-2 B / BR60 <400> 288 Met Ala Gln Val Ile Asn Thr Asn Ser Leu Ser Leu Leu Thr Gln Asn  1 5 10 15 Asn Leu Asn Lys Ser Gln Ser Ala Leu Gly Thr Ala Ile Glu Arg Leu             20 25 30 Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln         35 40 45 Ala Ile Ala Asn Arg Phe Thr Ala Asn Ile Lys Gly Leu Thr Gln Ala     50 55 60 Ser Arg Asn Ala Asn Asp Gly Ile Ser Ile Ala Gln Thr Thr Glu Gly 65 70 75 80 Ala Leu Asn Glu Ile Asn Asn Asn Leu Gln Arg Val Val Glu Leu Ala                 85 90 95 Val Gln Ser Ala Asn Ser Thr Asn Ser Gln Ser Asp Leu Asp Ser Ile             100 105 110 Gln Ala Glu Ile Thr Gln Arg Leu Asn Glu Ile Asp Arg Val Ser Gly         115 120 125 Gln Thr Gln Phe Asn Gly Val Lys Val Leu Ala Gln Asp Asn Thr Leu     130 135 140 Thr Ile Gln Val Gly Ala Asn Asp Gly Glu Thr Ile Asp Ile Asp Leu 145 150 155 160 Lys Gln Ile Asn Ser Gln Thr Leu Gly Leu Asp Ser Leu Asn Val Gln                 165 170 175 Lys Ala Tyr Asp Val Lys Asp Thr Ala Val Thr Thr Lys Ala Lys Gly             180 185 190 Thr Glu Thr Arg Gly Lys Leu Cys Pro Lys Cys Leu Asn Cys Thr Asp         195 200 205 Leu Asp Val Ala Leu Gly Arg Pro Lys Cys Thr Gly Lys Ile Pro Ser     210 215 220 Ala Arg Val Ser Ile Leu His Glu Val Arg Pro Val Thr Ser Gly Cys 225 230 235 240 Phe Pro Ile Met His Asp Arg Thr Lys Ile Arg Gln Leu Pro Asn Leu                 245 250 255 Leu Arg Gly Tyr Glu His Ile Arg Leu Ser Thr His Asn Val Ile Asn             260 265 270 Ala Glu Asn Ala Pro Gly Gly Pro Tyr Lys Ile Gly Thr Ser Gly Ser         275 280 285 Cys Pro Asn Ile Thr Asn Gly Asn Gly Phe Phe Ala Thr Met Ala Trp     290 295 300 Ala Val Pro Lys Asn Asp Lys Asn Lys Thr Ala Thr Asn Pro Leu Thr 305 310 315 320 Ile Glu Val Pro Tyr Ile Cys Thr Glu Gly Glu Asp Gln Ile Thr Val                 325 330 335 Trp Gly Phe His Ser Asp Asn Glu Thr Gln Met Ala Lys Leu Tyr Gly             340 345 350 Asp Ser Lys Pro Gln Lys Phe Thr Ser Ser Ala Asn Gly Val Thr Thr         355 360 365 His Tyr Val Ser Gln Ile Gly Gly Phe Pro Asn Gln Thr Glu Asp Gly     370 375 380 Gly Leu Pro Gln Ser Gly Arg Ile Val Val Asp Tyr Met Val Gln Lys 385 390 395 400 Ser Gly Lys Thr Gly Thr Ile Thr Tyr Gln Arg Gly Ile Leu Leu Pro                 405 410 415 Gln Lys Val Trp Cys Ala Ser Gly Arg Ser Ser Val Valle Lys Gly Ser             420 425 430 Val Val Ser Ala Asp Ala Lys Asn Ala Leu Ile Ala Gly Gly Val Asp         435 440 445 Ala Thr Asp Ala Asn Gly Ala Glu Leu Val Lys Met Ser Tyr Thr Asp     450 455 460 Lys Asn Gly Lys Thr Ile Gly Gly Gly Tyr Ala Leu Lys Ala Gly Asp 465 470 475 480 Lys Tyr Tyr Ala Ala Asp Tyr Asp Glu Ala Thr Gly Ala Ile Lys Ala                 485 490 495 Lys Thr Thr Ser Tyr Thr Ala Ala Asp Gly Thr Thr Lys Thr Ala Ala             500 505 510 Asn Gln Leu Gly Gly Val Asp Gly Lys Thr Glu Val Val Thr Ile Asp         515 520 525 Gly Lys Thr Tyr Asn Ala Ser Lys Ala Ala Gly His Asp Phe Lys Ala     530 535 540 Gln Pro Glu Leu Ala Glu Ala Ala Ala Lys Thr Thr Glu Asn Pro Leu 545 550 555 560 Gln Lys Ile Asp Ala Ala Leu Ala Gln Val Asp Ala Leu Arg Ser Asp                 565 570 575 Leu Gly Ala Val Gln Asn Arg Phe Asn Ser Ala Ile Thr Asn Leu Gly             580 585 590 Asn Thr Val Asn Asn Leu Ser Glu Ala Arg Ser Ser Ile Glu Asp Ser         595 600 605 Asp Tyr Ala Thr Glu Val Ser Asn Met Ser Arg Ala Gln Ile Leu Gln     610 615 620 Gln Ala Gly Thr Ser Val Leu Ala Gln Ala Asn Gln Val Pro Gln Asn 625 630 635 640 Val Leu Ser Leu Leu Ala Lys Gly Thr Glu Thr Arg Gly Lys Leu Cys                 645 650 655 Pro Lys Cys Leu Asn Cys Thr Asp Leu Asp Val Ala Leu Gly Arg Pro             660 665 670 Lys Cys Thr Gly Lys Ile Pro Ser Ala Arg Val Ser Ile Leu His Glu         675 680 685 Val Arg Pro Val Thr Ser Gly Cys Phe Pro Ile Met His Asp Arg Thr     690 695 700 Lys Ile Arg Gln Leu Pro Asn Leu Leu Arg Gly Tyr Glu His Ile Arg 705 710 715 720 Leu Ser Thr His Asn Val Ile Asn Ala Glu Asn Ala Pro Gly Gly Pro                 725 730 735 Tyr Lys Ile Gly Thr Ser Gly Ser Cys Pro Asn Ile Thr Asn Gly Asn             740 745 750 Gly Phe Phe Ala Thr Met Ala Trp Ala Val Pro Lys Asn Asp Lys Asn         755 760 765 Lys Thr Ala Thr Asn Pro Leu Thr Ile Glu Val Pro Tyr Ile Cys Thr     770 775 780 Glu Gly Glu Asp Gln Ile Thr Val Trp Gly Phe His Ser Asp Asn Glu 785 790 795 800 Thr Gln Met Ala Lys Leu Tyr Gly Asp Ser Lys Pro Gln Lys Phe Thr                 805 810 815 Ser Ser Ala Asn Gly Val Thr Thr His Tyr Val Ser Gln Ile Gly Gly             820 825 830 Phe Pro Asn Gln Thr Glu Asp Gly Gly Leu Pro Gln Ser Gly Arg Ile         835 840 845 Val Val Asp Tyr Met Val Gln Lys Ser Gly Lys Thr Gly Thr Ile Thr     850 855 860 Tyr Gln Arg Gly Ile Leu Leu Pro Gln Lys Val Trp Cys Ala Ser Gly 865 870 875 880 Arg Ser Lys Val Ile Lys Gly                 885

Claims (39)

(a) flagellin and
(b) a fusion protein comprising a fusion protein comprising at least one antigen fused to at least one loop of domain 3 of prasugin and having an isoelectric point greater than about 7.0, wherein the fusion protein activates toll-like receptor 5 . The composition of claim 1, wherein the isoelectric point of the antigen is at least one member selected from the group consisting of about 7.5, about 8.0, about 8.5, about 9.0, about 9.5, and about 10.0. 2. The composition of claim 1 wherein the porcelain lacks at least one of a portion of carboxy-domain 0 and a portion of amino-domain 0. 3. The composition of claim 1 further comprising an additional antigen fused to prazoline at a site distinct from the fusion of the antigen to the loop of domain 3 of the prazoline. The method according to claim 1, wherein the Prazelin is selected from the group consisting of Salmonella typhimurium prazoline, E-coli prazoline, S. muenchen praxelin, Yersinia praxelin, rugi labor (P. aeruginosa) PRA jelrin and L. monocytogenes to Ness composition comprising at least one member selected from the group consisting of (L. monocytogenes) jelrin plastic. 6. The composition of claim 5, wherein the prazelin is S. typhimurium prazoline. 7. The method of claim 6, wherein S. typhimurium prozelin is selected from the group consisting of SEQ ID NO. 1 &lt; / RTI &gt; and &lt; RTI ID = 0.0 &gt; 2. &Lt; / RTI &gt; 8. The composition of claim 7, wherein the S. typhimurium prozelin is SEQ ID NO: 2. 9. The composition of claim 8, wherein the antigen is fused between amino acid residue 277 and amino acid residue 278 of SEQ ID NO: 2. 9. The composition of claim 8, wherein the antigen is fused between amino acid residue 259 and amino acid residue 260 of SEQ ID NO: 2. 2. The composition of claim 1, wherein the antigen is an influenza virus antigen. 12. The composition of claim 11, wherein the influenza virus antigen is an influenza B virus antigen. 12. The composition of claim 11 wherein the influenza virus antigen is an influenza A antigen subtype and the influenza A antigen subtype is at least one member selected from the group consisting of H3, H7 and H9. 14. The composition of claim 13, wherein the influenza A antigen subtype is H3. 12. The composition of claim 11, wherein the influenza virus antigen is a hemagglutinin antigen. 16. The composition of claim 15, wherein the hemagglutinin antigen is at least one member selected from the group consisting of an influenza A virus hemagglutinin antigen and an influenza B virus hemagglutinin antigen. 16. The composition of claim 15, wherein the hemagglutinin antigen is part of a hemagglutinin antigen comprising at least a portion of a spherical head. 18. The composition of claim 17 wherein part of the hemagglutinin lacks transmembrane and cytoplasmic domains. 19. The composition of claim 18 wherein the portion of the hemagglutinin additionally lacks an HA2 subunit. 20. The composition of claim 19, wherein a portion of the spherical head has at least one 棺 -sheet on the bottom of a portion of the spherical head. 21. The composition of claim 20, wherein a portion of the spherical head further comprises at least one ß-sandwich on the bottom of a portion of the spherical head. 22. The composition of claim 21, wherein a portion of the spherical head further comprises at least two ß-strands at the bottom of a portion of the spherical head. 3. The composition of claim 1, further comprising an amino acid linker between the loop of domain 3 of Praseline and at least one of the amino-terminal or carboxy-terminal of the antigen. Each comprising at least three fusion proteins that activate toll-like receptor 5,
(a) the first fusion protein comprises a first plasine, and a first influenza A virus hemagglutinin antigen fused to a portion of the first flazelin and having an isoelectric point greater than about 6.0;
(b) a second fusion protein comprises a second influenza A virus hemagglutinin fused to a portion of a second plasine, and a second influenza A virus having an isoelectric point greater than about 7.0 and distinguishable from a first influenza A virus hemagglutinin antigen; Lutinin antigens;
(c) a third fusion protein comprising a first influenza B virus hemagglutinin antigen fused to at least one loop of domain 3 of the third plasine, and a third influenza virus having an isoelectric point greater than about 8.0 . 25. The composition of claim 24, further comprising at least one adjuvant. 25. The method of claim 24,
(a) the first influenza A virus hemagglutinin antigen comprises all or at least a portion of the HA1 subunit having at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head;
(b) a second influenza A virus hemagglutinin antigen binds at least a portion of a spherical head comprising at least one ß-sheet, at least one ß-sandwich and at least two ß-strands at the bottom of a portion of the spherical head Gt; HA1 &lt; / RTI &gt;
(c) a composition comprising a first or second influenza B virus hemagglutinin antigen comprising all or at least a portion of the HA1 subunit having at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head. 26. The method of claim 24, further comprising a fourth fusion protein that activates toll-like receptor 5, wherein the fourth fusion protein is fused to at least one loop of domain 3 of the fourth protein and has an isoelectric point greater than about 8.0 And a second influenza B virus hemagglutinin antigen distinct from the first influenza B virus hemagglutinin antigen. 28. The composition of claim 27, wherein the second influenza B virus hemagglutinin antigen comprises all or at least a portion of the HA1 subunit having at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head . A method of stimulating an immune response to an antigen in a subject, comprising administering to the subject a composition comprising at least one fusion protein that activates the toll-like receptor 5, wherein the fusion protein comprises a domain of prazoline and prazoline RTI ID = 0.0 &gt; 1, &lt; / RTI &gt; 3 and at least one antigen whose isoelectric point is greater than about 7.0. 29. The method of claim 29, wherein the dose of the fusion protein of the composition administered to the subject is about 1, about 2, about 3, about 4, about 5, about 6, about 7, From the group consisting of about 10 μg dose, about 15 μg dose, about 20 μg dose, about 25 μg dose, about 30 μg dose, about 35 μg dose, about 40 μg dose, about 45 μg dose and about 50 μg dose Selected at least one member. 30. The method of claim 29, wherein the composition is administered to a subject in a single dose. 30. The method of claim 29, wherein the composition is administered to the subject in multiple doses. 30. The method of claim 29, wherein the antigen is an influenza virus antigen. 30. The method of claim 29, wherein the influenza virus antigen is at least a portion of hemagglutinin. 30. The method of claim 29, wherein the composition comprises an adjuvant. A method of stimulating an immune response in a subject comprising administering to the subject a composition comprising at least three fusion proteins each activating the toll-like receptor 5,
(a) the first fusion protein comprises a first plasine, and a first influenza A virus hemagglutinin antigen fused to a portion of the first flazelin and having an isoelectric point greater than about 6.0;
(b) a second fusion protein comprises a second influenza A virus hemagglutinin fused to a portion of a second plasine, and a second influenza A virus having an isoelectric point greater than about 7.0 and distinguishable from a first influenza A virus hemagglutinin antigen; Lutinin antigens;
(c) the third fusion protein comprises a first influenza B virus hemagglutinin antigen which is fused to at least one loop of domain 3 of the third plasin, and of the third fragment, and has an isoelectric point greater than about 8.0 . 37. The method of claim 36,
(a) a first influenza A virus hemagglutinin antigen administered to a subject comprises all or at least a portion of the HA1 subunit having at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head ;
(b) a second influenza A virus hemagglutinin antigen being administered to a subject comprises a spherical head comprising at least one ß-sheet, at least one ß-sandwich and at least two ß-strands at the bottom of a part of the spherical head At least a portion of the HA1 subunit having at least a portion of the HA1 subunit;
(c) a first influenza B virus hemagglutinin antigen administered to the subject comprises all or at least a portion of the HA1 subunit having at least a portion of a spherical head comprising at least one [beta] -sheet at the bottom of the spherical head Way. 37. The method of claim 36, wherein the composition to be administered to the subject further comprises a fourth fusion protein that activates toll-like receptor 5, wherein the fourth fusion protein is fused to at least one loop of domain 3 of the fourth protein A second influenza B virus hemagglutinin antigen having an isoelectric point greater than about 8.0 and distinguished from a first influenza B virus hemagglutinin antigen. 39. The method of claim 38, wherein the second influenza B virus hemagglutinin antigen administered to the subject comprises at least a portion of the HA1 subunit having at least a portion of the spherical head comprising at least one [beta] -sheet at the bottom of the spherical head &Lt; / RTI &gt;

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